Copper in PDB 8q9x: The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
Protein crystallography data
The structure of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution, PDB code: 8q9x
was solved by
L.A.Varfolomeeva,
K.M.Polyakov,
N.S.Shipkov,
N.I.Dergousova,
K.M.Boyko,
T.V.Tikhonova,
V.O.Popov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
45.93 /
1.05
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
66.84,
96.57,
147.45,
90,
90,
90
|
|
R / Rfree (%)
|
10.8 /
12.6
|
Copper Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
11;
Binding sites:
The binding sites of Copper atom in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
(pdb code 8q9x). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 11 binding sites of Copper where determined in the
The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution, PDB code: 8q9x:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 1 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu605
b:9.8
occ:0.85
|
CU
|
A:CU609
|
1.7
|
13.1
|
0.1
|
|
O
|
A:HOH790
|
1.9
|
17.9
|
0.6
|
|
NE2
|
A:HIS171
|
1.9
|
10.2
|
1.0
|
|
NE2
|
A:HIS346
|
1.9
|
11.8
|
1.0
|
|
HE21
|
A:GLN347
|
2.0
|
11.0
|
0.1
|
|
OD1
|
A:ASP279
|
2.2
|
11.4
|
1.0
|
|
NE2
|
A:GLN347
|
2.7
|
10.5
|
0.1
|
|
HE21
|
A:GLN347
|
2.7
|
12.0
|
0.8
|
|
HE22
|
A:GLN347
|
2.8
|
11.0
|
0.1
|
|
CG
|
A:ASP279
|
2.9
|
10.4
|
1.0
|
|
CD2
|
A:HIS171
|
2.9
|
9.0
|
1.0
|
|
CD2
|
A:HIS346
|
2.9
|
11.1
|
1.0
|
|
OD2
|
A:ASP279
|
2.9
|
11.6
|
1.0
|
|
OE1
|
A:GLN347
|
3.0
|
12.9
|
0.8
|
|
CE1
|
A:HIS171
|
3.0
|
9.5
|
1.0
|
|
CE1
|
A:HIS346
|
3.0
|
12.6
|
1.0
|
|
HD2
|
A:HIS346
|
3.0
|
11.2
|
1.0
|
|
HD2
|
A:HIS171
|
3.0
|
9.5
|
1.0
|
|
HE1
|
A:HIS171
|
3.3
|
9.5
|
1.0
|
|
HE1
|
A:HIS346
|
3.3
|
11.2
|
1.0
|
|
NE2
|
A:GLN347
|
3.4
|
12.2
|
0.8
|
|
CD
|
A:GLN347
|
3.6
|
11.2
|
0.8
|
|
O
|
A:HOH970
|
3.7
|
12.1
|
1.0
|
|
O
|
A:HOH737
|
3.7
|
19.9
|
1.0
|
|
CD
|
A:GLN347
|
3.9
|
10.4
|
0.1
|
|
HG22
|
A:THR513
|
4.1
|
11.4
|
1.0
|
|
CG
|
A:HIS346
|
4.1
|
10.7
|
1.0
|
|
CG
|
A:HIS171
|
4.1
|
8.5
|
1.0
|
|
ND1
|
A:HIS346
|
4.1
|
12.1
|
1.0
|
|
HE1
|
A:HIS402
|
4.1
|
9.6
|
1.0
|
|
ND1
|
A:HIS171
|
4.2
|
9.6
|
1.0
|
|
HE22
|
A:GLN347
|
4.2
|
12.0
|
0.8
|
|
HG11
|
A:VAL170
|
4.3
|
9.0
|
1.0
|
|
CB
|
A:ASP279
|
4.3
|
9.7
|
1.0
|
|
HB
|
A:THR513
|
4.3
|
10.9
|
1.0
|
|
O
|
A:HOH781
|
4.4
|
11.0
|
1.0
|
|
HE2
|
A:HIS101
|
4.4
|
9.7
|
0.0
|
|
HG12
|
A:VAL170
|
4.4
|
9.0
|
1.0
|
|
OE1
|
A:GLN347
|
4.4
|
11.4
|
0.1
|
|
HG1
|
A:THR513
|
4.5
|
10.7
|
0.0
|
|
HD3
|
A:ARG295
|
4.6
|
9.8
|
0.5
|
|
HB3
|
A:ASP279
|
4.6
|
10.0
|
1.0
|
|
HA
|
A:GLN347
|
4.6
|
9.4
|
1.0
|
|
HD2
|
A:ARG295
|
4.7
|
9.8
|
0.5
|
|
CG1
|
A:VAL170
|
4.7
|
8.7
|
1.0
|
|
HB2
|
A:ALA280
|
4.8
|
8.4
|
1.0
|
|
HE1
|
A:HIS101
|
4.8
|
9.0
|
1.0
|
|
HG13
|
A:VAL170
|
4.8
|
9.0
|
1.0
|
|
HG2
|
A:GLN347
|
4.8
|
10.9
|
0.1
|
|
CE1
|
A:HIS402
|
4.8
|
10.1
|
1.0
|
|
HB2
|
A:ASP279
|
4.8
|
10.0
|
1.0
|
|
NE2
|
A:HIS101
|
4.8
|
10.1
|
1.0
|
|
CG2
|
A:THR513
|
4.9
|
11.5
|
1.0
|
|
HD1
|
A:HIS346
|
4.9
|
11.5
|
0.0
|
|
HD1
|
A:HIS171
|
4.9
|
9.2
|
0.0
|
|
CG
|
A:GLN347
|
5.0
|
10.6
|
0.8
|
|
CB
|
A:THR513
|
5.0
|
9.8
|
1.0
|
|
CG
|
A:GLN347
|
5.0
|
9.7
|
0.1
|
|
Copper binding site 2 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 2 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu606
b:9.5
occ:0.70
|
CU
|
A:CU606
|
0.0
|
9.5
|
0.7
|
|
CU
|
A:CU606
|
0.6
|
20.1
|
0.3
|
|
O2
|
A:OXY604
|
1.8
|
13.1
|
0.7
|
|
NE2
|
A:HIS100
|
2.0
|
8.6
|
1.0
|
|
ND1
|
A:HIS493
|
2.1
|
10.2
|
1.0
|
|
O
|
A:HOH846
|
2.2
|
10.8
|
1.0
|
|
O
|
A:HOH737
|
2.5
|
19.9
|
1.0
|
|
HB3
|
A:HIS493
|
2.9
|
8.8
|
1.0
|
|
O1
|
A:OXY604
|
3.0
|
13.1
|
0.7
|
|
HZ3
|
A:LYS68
|
3.0
|
10.6
|
1.0
|
|
CE1
|
A:HIS100
|
3.0
|
8.8
|
1.0
|
|
CG
|
A:HIS493
|
3.1
|
9.0
|
1.0
|
|
CD2
|
A:HIS100
|
3.1
|
8.5
|
1.0
|
|
HE1
|
A:HIS100
|
3.1
|
8.8
|
1.0
|
|
CE1
|
A:HIS493
|
3.1
|
10.4
|
1.0
|
|
HE2
|
A:HIS101
|
3.2
|
9.7
|
0.0
|
|
HD2
|
A:HIS100
|
3.3
|
8.8
|
1.0
|
|
CB
|
A:HIS493
|
3.3
|
8.4
|
1.0
|
|
HE1
|
A:HIS493
|
3.3
|
10.1
|
1.0
|
|
HB2
|
A:HIS493
|
3.4
|
8.8
|
1.0
|
|
NZ
|
A:LYS68
|
3.8
|
10.5
|
1.0
|
|
NE2
|
A:HIS101
|
3.8
|
10.1
|
1.0
|
|
HZ1
|
A:LYS68
|
3.8
|
10.6
|
1.0
|
|
HG3
|
A:PRO256
|
4.0
|
11.0
|
1.0
|
|
HE1
|
A:HIS101
|
4.1
|
9.0
|
1.0
|
|
ND1
|
A:HIS100
|
4.1
|
8.6
|
1.0
|
|
O
|
A:HOH1083
|
4.2
|
11.5
|
1.0
|
|
CG
|
A:HIS100
|
4.2
|
8.2
|
1.0
|
|
CD2
|
A:HIS493
|
4.2
|
9.6
|
1.0
|
|
HD3
|
A:LYS68
|
4.2
|
9.6
|
1.0
|
|
NE2
|
A:HIS493
|
4.2
|
10.4
|
1.0
|
|
CE1
|
A:HIS101
|
4.2
|
9.5
|
1.0
|
|
HZ2
|
A:LYS68
|
4.3
|
10.6
|
1.0
|
|
OE1
|
A:GLU253
|
4.3
|
10.0
|
1.0
|
|
O
|
A:HOH970
|
4.4
|
12.1
|
1.0
|
|
O
|
A:HOH790
|
4.4
|
17.9
|
0.6
|
|
HD3
|
A:PRO256
|
4.5
|
10.6
|
1.0
|
|
CU
|
A:CU607
|
4.7
|
10.1
|
1.0
|
|
CE
|
A:LYS68
|
4.7
|
9.4
|
1.0
|
|
CG
|
A:PRO256
|
4.7
|
11.3
|
1.0
|
|
HG2
|
A:PRO256
|
4.7
|
11.0
|
1.0
|
|
CD2
|
A:HIS101
|
4.7
|
9.2
|
1.0
|
|
HE1
|
A:HIS447
|
4.8
|
11.0
|
1.0
|
|
HE2
|
A:LYS68
|
4.8
|
9.6
|
1.0
|
|
HG13
|
A:VAL170
|
4.8
|
9.0
|
1.0
|
|
CA
|
A:HIS493
|
4.8
|
7.7
|
1.0
|
|
CD
|
A:LYS68
|
4.9
|
9.5
|
1.0
|
|
HD1
|
A:HIS100
|
4.9
|
8.4
|
0.0
|
|
HH
|
A:TYR129
|
4.9
|
10.6
|
0.0
|
|
HD2
|
A:HIS101
|
5.0
|
9.0
|
1.0
|
|
Copper binding site 3 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 3 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu606
b:20.1
occ:0.30
|
CU
|
A:CU606
|
0.0
|
20.1
|
0.3
|
|
CU
|
A:CU606
|
0.6
|
9.5
|
0.7
|
|
ND1
|
A:HIS493
|
1.8
|
10.2
|
1.0
|
|
NE2
|
A:HIS100
|
1.9
|
8.6
|
1.0
|
|
O
|
A:HOH846
|
2.1
|
10.8
|
1.0
|
|
O2
|
A:OXY604
|
2.3
|
13.1
|
0.7
|
|
HZ3
|
A:LYS68
|
2.4
|
10.6
|
1.0
|
|
CE1
|
A:HIS493
|
2.7
|
10.4
|
1.0
|
|
CD2
|
A:HIS100
|
2.8
|
8.5
|
1.0
|
|
CG
|
A:HIS493
|
2.8
|
9.0
|
1.0
|
|
HE1
|
A:HIS493
|
2.9
|
10.1
|
1.0
|
|
CE1
|
A:HIS100
|
2.9
|
8.8
|
1.0
|
|
HD2
|
A:HIS100
|
3.0
|
8.8
|
1.0
|
|
HB3
|
A:HIS493
|
3.1
|
8.8
|
1.0
|
|
O
|
A:HOH737
|
3.1
|
19.9
|
1.0
|
|
NZ
|
A:LYS68
|
3.2
|
10.5
|
1.0
|
|
HE1
|
A:HIS100
|
3.2
|
8.8
|
1.0
|
|
HB2
|
A:HIS493
|
3.2
|
8.8
|
1.0
|
|
HZ1
|
A:LYS68
|
3.3
|
10.6
|
1.0
|
|
CB
|
A:HIS493
|
3.3
|
8.4
|
1.0
|
|
O1
|
A:OXY604
|
3.4
|
13.1
|
0.7
|
|
HE2
|
A:HIS101
|
3.6
|
9.7
|
0.0
|
|
HD3
|
A:LYS68
|
3.6
|
9.6
|
1.0
|
|
HZ2
|
A:LYS68
|
3.7
|
10.6
|
1.0
|
|
NE2
|
A:HIS493
|
3.9
|
10.4
|
1.0
|
|
CD2
|
A:HIS493
|
3.9
|
9.6
|
1.0
|
|
CG
|
A:HIS100
|
4.0
|
8.2
|
1.0
|
|
ND1
|
A:HIS100
|
4.0
|
8.6
|
1.0
|
|
CE
|
A:LYS68
|
4.1
|
9.4
|
1.0
|
|
OE1
|
A:GLU253
|
4.1
|
10.0
|
1.0
|
|
NE2
|
A:HIS101
|
4.1
|
10.1
|
1.0
|
|
HE2
|
A:LYS68
|
4.2
|
9.6
|
1.0
|
|
HG3
|
A:PRO256
|
4.2
|
11.0
|
1.0
|
|
CD
|
A:LYS68
|
4.3
|
9.5
|
1.0
|
|
HD3
|
A:PRO256
|
4.4
|
10.6
|
1.0
|
|
O
|
A:HOH1083
|
4.5
|
11.5
|
1.0
|
|
HE1
|
A:HIS101
|
4.6
|
9.0
|
1.0
|
|
HH
|
A:TYR129
|
4.6
|
10.6
|
0.0
|
|
HE2
|
A:HIS493
|
4.6
|
9.7
|
0.0
|
|
CE1
|
A:HIS101
|
4.6
|
9.5
|
1.0
|
|
HD2
|
A:LYS68
|
4.6
|
9.6
|
1.0
|
|
OH
|
A:TYR129
|
4.6
|
10.8
|
1.0
|
|
HG2
|
A:PRO256
|
4.7
|
11.0
|
1.0
|
|
OE2
|
A:GLU253
|
4.7
|
10.2
|
1.0
|
|
CG
|
A:PRO256
|
4.8
|
11.3
|
1.0
|
|
CA
|
A:HIS493
|
4.8
|
7.7
|
1.0
|
|
HD2
|
A:HIS493
|
4.8
|
10.1
|
1.0
|
|
HD1
|
A:HIS100
|
4.8
|
8.4
|
0.0
|
|
HE1
|
A:HIS447
|
4.8
|
11.0
|
1.0
|
|
O
|
A:HOH970
|
4.9
|
12.1
|
1.0
|
|
CD
|
A:GLU253
|
4.9
|
9.2
|
1.0
|
|
HE21
|
A:GLN121
|
4.9
|
10.1
|
1.0
|
|
HE3
|
A:LYS68
|
5.0
|
9.6
|
1.0
|
|
Copper binding site 4 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 4 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu607
b:10.1
occ:1.00
|
O1
|
A:OXY604
|
1.9
|
13.1
|
0.7
|
|
NE2
|
A:HIS402
|
2.0
|
9.5
|
1.0
|
|
ND1
|
A:HIS447
|
2.0
|
9.2
|
1.0
|
|
CE1
|
A:HIS447
|
2.9
|
9.2
|
1.0
|
|
CE1
|
A:HIS402
|
2.9
|
10.1
|
1.0
|
|
HZ
|
A:PHE401
|
3.0
|
11.3
|
1.0
|
|
HE1
|
A:HIS447
|
3.0
|
11.0
|
1.0
|
|
CD2
|
A:HIS402
|
3.1
|
8.7
|
1.0
|
|
O2
|
A:OXY604
|
3.1
|
13.1
|
0.7
|
|
HE1
|
A:HIS402
|
3.1
|
9.6
|
1.0
|
|
HE1
|
A:PHE401
|
3.1
|
11.3
|
1.0
|
|
HB3
|
A:HIS447
|
3.1
|
8.8
|
1.0
|
|
CG
|
A:HIS447
|
3.2
|
8.5
|
1.0
|
|
HD2
|
A:HIS402
|
3.3
|
9.6
|
1.0
|
|
CZ
|
A:PHE401
|
3.3
|
12.2
|
1.0
|
|
HB3
|
A:HIS493
|
3.4
|
8.8
|
1.0
|
|
CE1
|
A:PHE401
|
3.4
|
11.0
|
1.0
|
|
CB
|
A:HIS447
|
3.6
|
8.5
|
1.0
|
|
HA
|
A:HIS447
|
3.7
|
9.6
|
1.0
|
|
HA
|
A:HIS493
|
3.7
|
8.4
|
1.0
|
|
HE22
|
A:GLN347
|
3.8
|
12.0
|
0.8
|
|
O
|
A:HIS493
|
3.9
|
10.3
|
1.0
|
|
HE21
|
A:GLN347
|
3.9
|
12.0
|
0.8
|
|
O
|
A:HOH790
|
4.0
|
17.9
|
0.6
|
|
CB
|
A:HIS493
|
4.1
|
8.4
|
1.0
|
|
ND1
|
A:HIS402
|
4.1
|
10.0
|
1.0
|
|
NE2
|
A:HIS447
|
4.1
|
9.3
|
1.0
|
|
HG23
|
A:THR448
|
4.1
|
9.7
|
1.0
|
|
CA
|
A:HIS447
|
4.2
|
8.0
|
1.0
|
|
CG
|
A:HIS402
|
4.2
|
8.3
|
1.0
|
|
NE2
|
A:GLN347
|
4.2
|
12.2
|
0.8
|
|
CD2
|
A:HIS447
|
4.2
|
8.7
|
1.0
|
|
CA
|
A:HIS493
|
4.3
|
7.7
|
1.0
|
|
CG
|
A:HIS493
|
4.3
|
9.0
|
1.0
|
|
CE2
|
A:PHE401
|
4.3
|
13.4
|
1.0
|
|
CD1
|
A:PHE401
|
4.4
|
9.8
|
1.0
|
|
HG3
|
A:PRO256
|
4.4
|
11.0
|
1.0
|
|
HE1
|
A:HIS101
|
4.4
|
9.0
|
1.0
|
|
HB2
|
A:HIS447
|
4.5
|
8.8
|
1.0
|
|
C
|
A:HIS493
|
4.5
|
8.3
|
1.0
|
|
HE22
|
A:GLN347
|
4.6
|
11.0
|
0.1
|
|
ND1
|
A:HIS493
|
4.6
|
10.2
|
1.0
|
|
HE2
|
A:PHE401
|
4.7
|
11.3
|
1.0
|
|
CU
|
A:CU606
|
4.7
|
9.5
|
0.7
|
|
CD2
|
A:HIS493
|
4.7
|
9.6
|
1.0
|
|
HD1
|
A:PHE401
|
4.8
|
11.3
|
1.0
|
|
C
|
A:HIS447
|
4.8
|
7.8
|
1.0
|
|
HD1
|
A:HIS402
|
4.8
|
9.7
|
0.0
|
|
HE2
|
A:HIS447
|
4.9
|
8.8
|
0.0
|
|
HG2
|
A:PRO256
|
4.9
|
11.0
|
1.0
|
|
HB3
|
A:PRO256
|
4.9
|
11.2
|
1.0
|
|
HB2
|
A:HIS493
|
4.9
|
8.8
|
1.0
|
|
HD2
|
A:HIS493
|
5.0
|
10.1
|
1.0
|
|
H
|
A:THR448
|
5.0
|
8.8
|
1.0
|
|
Copper binding site 5 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 5 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu608
b:21.8
occ:0.60
|
ND1
|
A:HIS44
|
1.9
|
26.1
|
1.0
|
|
N
|
A:HIS44
|
2.0
|
28.1
|
1.0
|
|
N
|
A:GLY43
|
2.1
|
35.0
|
1.0
|
|
H
|
A:GLY43
|
2.4
|
34.3
|
1.0
|
|
CG
|
A:HIS44
|
2.8
|
24.1
|
1.0
|
|
CE1
|
A:HIS44
|
2.9
|
30.8
|
1.0
|
|
H
|
A:MET45
|
2.9
|
23.4
|
1.0
|
|
C
|
A:GLY43
|
3.0
|
29.2
|
1.0
|
|
CA
|
A:HIS44
|
3.0
|
26.2
|
1.0
|
|
CA
|
A:GLY43
|
3.1
|
35.1
|
1.0
|
|
HE1
|
A:HIS44
|
3.2
|
29.0
|
1.0
|
|
CB
|
A:HIS44
|
3.2
|
25.1
|
1.0
|
|
HB3
|
A:HIS44
|
3.2
|
24.1
|
1.0
|
|
HA2
|
A:GLY43
|
3.5
|
32.5
|
1.0
|
|
N
|
A:MET45
|
3.6
|
21.3
|
1.0
|
|
C
|
A:HIS44
|
3.8
|
26.1
|
1.0
|
|
HA
|
A:HIS44
|
3.8
|
23.1
|
1.0
|
|
HA3
|
A:GLY43
|
3.8
|
32.5
|
1.0
|
|
CD2
|
A:HIS44
|
3.9
|
28.2
|
1.0
|
|
NE2
|
A:HIS44
|
3.9
|
28.5
|
1.0
|
|
O
|
A:GLY43
|
4.1
|
34.6
|
1.0
|
|
HB2
|
A:HIS44
|
4.1
|
24.1
|
1.0
|
|
HB2
|
A:MET45
|
4.6
|
29.7
|
1.0
|
|
HD2
|
A:HIS44
|
4.8
|
27.3
|
1.0
|
|
CA
|
A:MET45
|
4.9
|
24.0
|
1.0
|
|
O
|
A:HIS44
|
4.9
|
26.5
|
1.0
|
|
Copper binding site 6 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 6 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu609
b:13.1
occ:0.15
|
HE21
|
A:GLN347
|
1.4
|
11.0
|
0.1
|
|
CU
|
A:CU605
|
1.7
|
9.8
|
0.8
|
|
OE1
|
A:GLN347
|
1.8
|
12.9
|
0.8
|
|
NE2
|
A:GLN347
|
1.9
|
10.5
|
0.1
|
|
NE2
|
A:HIS171
|
1.9
|
10.2
|
1.0
|
|
HE1
|
A:HIS171
|
2.2
|
9.5
|
1.0
|
|
O
|
A:HOH790
|
2.3
|
17.9
|
0.6
|
|
CE1
|
A:HIS171
|
2.3
|
9.5
|
1.0
|
|
HE22
|
A:GLN347
|
2.3
|
11.0
|
0.1
|
|
HE21
|
A:GLN347
|
2.4
|
12.0
|
0.8
|
|
CD
|
A:GLN347
|
2.6
|
11.2
|
0.8
|
|
CD
|
A:GLN347
|
2.8
|
10.4
|
0.1
|
|
NE2
|
A:GLN347
|
2.8
|
12.2
|
0.8
|
|
HB
|
A:THR513
|
2.8
|
10.9
|
1.0
|
|
OE1
|
A:GLN347
|
3.0
|
11.4
|
0.1
|
|
NE2
|
A:HIS346
|
3.0
|
11.8
|
1.0
|
|
HE1
|
A:HIS402
|
3.0
|
9.6
|
1.0
|
|
CD2
|
A:HIS171
|
3.2
|
9.0
|
1.0
|
|
OD1
|
A:ASP279
|
3.2
|
11.4
|
1.0
|
|
HG22
|
A:THR513
|
3.2
|
11.4
|
1.0
|
|
HG1
|
A:THR513
|
3.3
|
10.7
|
0.0
|
|
CB
|
A:THR513
|
3.5
|
9.8
|
1.0
|
|
ND1
|
A:HIS171
|
3.6
|
9.6
|
1.0
|
|
HE22
|
A:GLN347
|
3.6
|
12.0
|
0.8
|
|
HD2
|
A:HIS346
|
3.6
|
11.2
|
1.0
|
|
CE1
|
A:HIS402
|
3.6
|
10.1
|
1.0
|
|
CD2
|
A:HIS346
|
3.7
|
11.1
|
1.0
|
|
HD2
|
A:HIS171
|
3.7
|
9.5
|
1.0
|
|
OG1
|
A:THR513
|
3.7
|
11.4
|
1.0
|
|
CG2
|
A:THR513
|
3.8
|
11.5
|
1.0
|
|
HD1
|
A:HIS402
|
3.9
|
9.7
|
0.0
|
|
HA
|
A:GLN347
|
4.0
|
9.4
|
1.0
|
|
CG
|
A:HIS171
|
4.0
|
8.5
|
1.0
|
|
CE1
|
A:HIS346
|
4.0
|
12.6
|
1.0
|
|
ND1
|
A:HIS402
|
4.0
|
10.0
|
1.0
|
|
CG
|
A:GLN347
|
4.1
|
10.6
|
0.8
|
|
CG
|
A:GLN347
|
4.1
|
9.7
|
0.1
|
|
HG21
|
A:THR513
|
4.2
|
11.4
|
1.0
|
|
HD1
|
A:HIS171
|
4.2
|
9.2
|
0.0
|
|
CG
|
A:ASP279
|
4.2
|
10.4
|
1.0
|
|
HE1
|
A:HIS346
|
4.3
|
11.2
|
1.0
|
|
HG2
|
A:GLN347
|
4.3
|
10.9
|
0.1
|
|
O
|
A:HOH1068
|
4.3
|
13.3
|
1.0
|
|
O
|
A:HOH781
|
4.4
|
11.0
|
1.0
|
|
HE1
|
A:HIS101
|
4.4
|
9.0
|
1.0
|
|
OD2
|
A:ASP279
|
4.5
|
11.6
|
1.0
|
|
HG2
|
A:GLN347
|
4.5
|
10.9
|
0.8
|
|
HG3
|
A:GLN347
|
4.6
|
10.9
|
0.8
|
|
O
|
A:HOH737
|
4.6
|
19.9
|
1.0
|
|
HG23
|
A:THR513
|
4.6
|
11.4
|
1.0
|
|
NE2
|
A:HIS402
|
4.6
|
9.5
|
1.0
|
|
HB2
|
A:ALA280
|
4.7
|
8.4
|
1.0
|
|
HB3
|
A:GLN347
|
4.7
|
10.8
|
1.0
|
|
HG3
|
A:GLN347
|
4.7
|
10.9
|
0.1
|
|
CA
|
A:GLN347
|
4.8
|
8.7
|
1.0
|
|
CB
|
A:GLN347
|
4.8
|
10.0
|
1.0
|
|
O
|
A:THR513
|
4.8
|
10.8
|
1.0
|
|
CG
|
A:HIS346
|
4.8
|
10.7
|
1.0
|
|
CA
|
A:THR513
|
4.8
|
9.5
|
1.0
|
|
CE1
|
A:HIS101
|
4.9
|
9.5
|
1.0
|
|
HE2
|
A:HIS101
|
4.9
|
9.7
|
0.0
|
|
ND1
|
A:HIS346
|
4.9
|
12.1
|
1.0
|
|
Copper binding site 7 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 7 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu602
b:11.0
occ:1.00
|
NE2
|
B:HIS171
|
1.9
|
10.1
|
1.0
|
|
NE2
|
B:HIS346
|
2.0
|
10.8
|
1.0
|
|
O
|
B:HOH878
|
2.1
|
11.5
|
0.3
|
|
O
|
B:HOH900
|
2.1
|
14.9
|
0.3
|
|
OD2
|
B:ASP279
|
2.4
|
11.5
|
1.0
|
|
OD1
|
B:ASP279
|
2.5
|
12.0
|
1.0
|
|
CG
|
B:ASP279
|
2.8
|
11.0
|
1.0
|
|
CD2
|
B:HIS171
|
2.9
|
9.6
|
1.0
|
|
CD2
|
B:HIS346
|
3.0
|
11.6
|
1.0
|
|
CE1
|
B:HIS171
|
3.0
|
10.1
|
1.0
|
|
CE1
|
B:HIS346
|
3.0
|
11.6
|
1.0
|
|
HD2
|
B:HIS171
|
3.1
|
10.2
|
1.0
|
|
HD2
|
B:HIS346
|
3.1
|
25.3
|
1.0
|
|
HE1
|
B:HIS171
|
3.2
|
10.2
|
1.0
|
|
HE1
|
B:HIS346
|
3.2
|
25.3
|
1.0
|
|
HG1
|
B:THR513
|
3.6
|
11.3
|
0.0
|
|
CG
|
B:HIS171
|
4.1
|
9.2
|
1.0
|
|
ND1
|
B:HIS346
|
4.1
|
11.0
|
1.0
|
|
ND1
|
B:HIS171
|
4.1
|
9.7
|
1.0
|
|
CG
|
B:HIS346
|
4.1
|
10.1
|
1.0
|
|
CB
|
B:ASP279
|
4.3
|
10.6
|
1.0
|
|
OG1
|
B:THR513
|
4.3
|
11.9
|
1.0
|
|
O
|
B:HOH879
|
4.3
|
12.1
|
0.5
|
|
O
|
B:HOH756
|
4.4
|
11.9
|
1.0
|
|
HB2
|
B:PHE401
|
4.5
|
12.3
|
1.0
|
|
HG11
|
B:VAL170
|
4.5
|
10.5
|
1.0
|
|
HD2
|
B:ARG295
|
4.6
|
10.8
|
1.0
|
|
O
|
B:PHE401
|
4.6
|
12.5
|
1.0
|
|
O
|
B:HOH735
|
4.6
|
11.4
|
1.0
|
|
HG12
|
B:VAL170
|
4.6
|
10.5
|
1.0
|
|
HB2
|
B:ASP279
|
4.6
|
10.7
|
1.0
|
|
HB3
|
B:ASP279
|
4.6
|
10.7
|
1.0
|
|
HE21
|
B:GLN347
|
4.6
|
11.6
|
1.0
|
|
HE1
|
B:HIS402
|
4.7
|
11.7
|
1.0
|
|
HB2
|
B:ALA280
|
4.7
|
9.9
|
1.0
|
|
HD1
|
B:HIS346
|
4.9
|
10.5
|
0.0
|
|
HB
|
B:THR513
|
4.9
|
11.4
|
1.0
|
|
HD1
|
B:HIS171
|
4.9
|
9.5
|
0.0
|
|
O
|
B:HOH855
|
4.9
|
23.8
|
0.5
|
|
CG1
|
B:VAL170
|
4.9
|
10.4
|
1.0
|
|
HE2
|
B:HIS101
|
5.0
|
11.0
|
0.0
|
|
Copper binding site 8 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 8 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu603
b:8.9
occ:0.35
|
CU
|
B:CU603
|
0.0
|
8.9
|
0.3
|
|
CU
|
B:CU603
|
1.0
|
13.1
|
0.7
|
|
ND1
|
B:HIS493
|
1.9
|
11.3
|
1.0
|
|
O
|
B:HOH711
|
1.9
|
8.7
|
0.3
|
|
NE2
|
B:HIS100
|
2.0
|
9.6
|
1.0
|
|
NZ
|
B:LYS68
|
2.2
|
14.8
|
1.0
|
|
O
|
B:HOH887
|
2.2
|
16.0
|
1.0
|
|
HZ1
|
B:LYS68
|
2.5
|
14.8
|
0.0
|
|
HZ2
|
B:LYS68
|
2.6
|
14.8
|
0.0
|
|
CE1
|
B:HIS493
|
2.8
|
11.1
|
1.0
|
|
CD2
|
B:HIS100
|
2.8
|
9.0
|
1.0
|
|
HD2
|
B:HIS100
|
2.9
|
9.5
|
1.0
|
|
HE1
|
B:HIS493
|
2.9
|
10.4
|
1.0
|
|
CG
|
B:HIS493
|
3.0
|
8.7
|
1.0
|
|
HD3
|
B:LYS68
|
3.0
|
11.1
|
1.0
|
|
CE1
|
B:HIS100
|
3.0
|
9.1
|
1.0
|
|
CE
|
B:LYS68
|
3.2
|
11.9
|
1.0
|
|
HB2
|
B:HIS493
|
3.2
|
9.5
|
1.0
|
|
O
|
B:HOH1125
|
3.3
|
24.4
|
0.5
|
|
O
|
B:HOH855
|
3.3
|
23.8
|
0.5
|
|
HE1
|
B:HIS100
|
3.4
|
9.5
|
1.0
|
|
HE2
|
B:LYS68
|
3.4
|
9.8
|
1.0
|
|
CB
|
B:HIS493
|
3.4
|
9.2
|
1.0
|
|
HB3
|
B:HIS493
|
3.4
|
9.5
|
1.0
|
|
CD
|
B:LYS68
|
3.5
|
11.1
|
1.0
|
|
HH
|
B:TYR129
|
3.8
|
13.4
|
0.0
|
|
HD2
|
B:LYS68
|
3.9
|
11.1
|
1.0
|
|
NE2
|
B:HIS493
|
3.9
|
10.0
|
1.0
|
|
CG
|
B:HIS100
|
3.9
|
8.6
|
1.0
|
|
CD2
|
B:HIS493
|
4.0
|
9.3
|
1.0
|
|
OH
|
B:TYR129
|
4.0
|
15.0
|
0.6
|
|
O
|
B:HOH879
|
4.0
|
12.1
|
0.5
|
|
HE3
|
B:LYS68
|
4.0
|
9.8
|
1.0
|
|
ND1
|
B:HIS100
|
4.0
|
8.9
|
1.0
|
|
O
|
B:HOH1205
|
4.2
|
24.1
|
0.5
|
|
HE2
|
B:HIS101
|
4.2
|
11.0
|
0.0
|
|
OE1
|
B:GLU253
|
4.2
|
13.4
|
1.0
|
|
OE1
|
B:GLN121
|
4.3
|
13.4
|
1.0
|
|
O
|
B:HOH1148
|
4.4
|
19.8
|
0.3
|
|
OH
|
B:TYR129
|
4.4
|
22.9
|
0.4
|
|
HH
|
B:TYR129
|
4.4
|
16.9
|
0.0
|
|
HE2
|
B:HIS493
|
4.6
|
9.6
|
0.0
|
|
O
|
B:HOH1039
|
4.6
|
14.6
|
1.0
|
|
NE2
|
B:HIS101
|
4.7
|
11.6
|
1.0
|
|
HD2
|
B:HIS493
|
4.8
|
10.4
|
1.0
|
|
HD1
|
B:HIS100
|
4.9
|
8.7
|
0.0
|
|
CG
|
B:LYS68
|
4.9
|
10.8
|
1.0
|
|
HA
|
B:HIS100
|
4.9
|
9.5
|
1.0
|
|
HG2
|
B:LYS68
|
4.9
|
9.8
|
1.0
|
|
CA
|
B:HIS493
|
4.9
|
8.2
|
1.0
|
|
O
|
B:HOH1253
|
5.0
|
20.5
|
0.5
|
|
Copper binding site 9 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 9 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu603
b:13.1
occ:0.65
|
CU
|
B:CU603
|
0.0
|
13.1
|
0.7
|
|
O
|
B:HOH711
|
0.9
|
8.7
|
0.3
|
|
CU
|
B:CU603
|
1.0
|
8.9
|
0.3
|
|
NE2
|
B:HIS100
|
2.0
|
9.6
|
1.0
|
|
ND1
|
B:HIS493
|
2.0
|
11.3
|
1.0
|
|
O
|
B:HOH887
|
2.2
|
16.0
|
1.0
|
|
O
|
B:HOH855
|
2.3
|
23.8
|
0.5
|
|
O
|
B:HOH1125
|
2.3
|
24.4
|
0.5
|
|
HB3
|
B:HIS493
|
2.9
|
9.5
|
1.0
|
|
CG
|
B:HIS493
|
3.0
|
8.7
|
1.0
|
|
CE1
|
B:HIS100
|
3.0
|
9.1
|
1.0
|
|
CD2
|
B:HIS100
|
3.0
|
9.0
|
1.0
|
|
CE1
|
B:HIS493
|
3.1
|
11.1
|
1.0
|
|
HB2
|
B:HIS493
|
3.1
|
9.5
|
1.0
|
|
O
|
B:HOH879
|
3.1
|
12.1
|
0.5
|
|
NZ
|
B:LYS68
|
3.2
|
14.8
|
1.0
|
|
HD2
|
B:HIS100
|
3.2
|
9.5
|
1.0
|
|
HE1
|
B:HIS100
|
3.2
|
9.5
|
1.0
|
|
CB
|
B:HIS493
|
3.2
|
9.2
|
1.0
|
|
HE1
|
B:HIS493
|
3.3
|
10.4
|
1.0
|
|
HZ1
|
B:LYS68
|
3.4
|
14.8
|
0.0
|
|
HE2
|
B:HIS101
|
3.4
|
11.0
|
0.0
|
|
HZ2
|
B:LYS68
|
3.5
|
14.8
|
0.0
|
|
O
|
B:HOH1148
|
3.6
|
19.8
|
0.3
|
|
O
|
B:HOH1205
|
3.7
|
24.1
|
0.5
|
|
HD3
|
B:LYS68
|
3.8
|
11.1
|
1.0
|
|
NE2
|
B:HIS101
|
3.9
|
11.6
|
1.0
|
|
OE1
|
B:GLU253
|
4.1
|
13.4
|
1.0
|
|
CD2
|
B:HIS493
|
4.1
|
9.3
|
1.0
|
|
ND1
|
B:HIS100
|
4.1
|
8.9
|
1.0
|
|
CG
|
B:HIS100
|
4.2
|
8.6
|
1.0
|
|
NE2
|
B:HIS493
|
4.2
|
10.0
|
1.0
|
|
CE
|
B:LYS68
|
4.2
|
11.9
|
1.0
|
|
HE1
|
B:HIS101
|
4.3
|
10.5
|
1.0
|
|
HH
|
B:TYR129
|
4.3
|
13.4
|
0.0
|
|
HE2
|
B:LYS68
|
4.4
|
9.8
|
1.0
|
|
CE1
|
B:HIS101
|
4.4
|
10.7
|
1.0
|
|
CD
|
B:LYS68
|
4.5
|
11.1
|
1.0
|
|
OH
|
B:TYR129
|
4.6
|
15.0
|
0.6
|
|
O
|
B:HOH1253
|
4.7
|
20.5
|
0.5
|
|
OE2
|
B:GLU253
|
4.7
|
13.2
|
1.0
|
|
CA
|
B:HIS493
|
4.7
|
8.2
|
1.0
|
|
HD2
|
B:LYS68
|
4.7
|
11.1
|
1.0
|
|
CD
|
B:GLU253
|
4.8
|
12.0
|
1.0
|
|
CD2
|
B:HIS101
|
4.8
|
10.5
|
1.0
|
|
OE1
|
B:GLN121
|
4.9
|
13.4
|
1.0
|
|
HH
|
B:TYR129
|
4.9
|
16.9
|
0.0
|
|
HD1
|
B:HIS100
|
4.9
|
8.7
|
0.0
|
|
HE1
|
B:HIS447
|
4.9
|
20.5
|
1.0
|
|
HE2
|
B:HIS493
|
5.0
|
9.6
|
0.0
|
|
HD2
|
B:HIS493
|
5.0
|
10.4
|
1.0
|
|
Copper binding site 10 out
of 11 in 8q9x
Go back to
Copper Binding Sites List in 8q9x
Copper binding site 10 out
of 11 in the The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of The Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum with Molecular Oxygen at 1.05 A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu604
b:10.5
occ:0.65
|
CU
|
B:CU604
|
0.0
|
10.5
|
0.7
|
|
CU
|
B:CU604
|
0.7
|
15.4
|
0.3
|
|
ND1
|
B:HIS447
|
1.8
|
10.4
|
1.0
|
|
NE2
|
B:HIS402
|
1.9
|
12.7
|
1.0
|
|
O
|
B:HOH1148
|
2.5
|
19.8
|
0.3
|
|
HB3
|
B:HIS447
|
2.7
|
10.1
|
1.0
|
|
CG
|
B:HIS447
|
2.8
|
9.5
|
1.0
|
|
CD2
|
B:HIS402
|
2.9
|
10.1
|
1.0
|
|
CE1
|
B:HIS447
|
2.9
|
10.1
|
1.0
|
|
HA
|
B:HIS447
|
2.9
|
9.5
|
1.0
|
|
CE1
|
B:HIS402
|
2.9
|
14.8
|
1.0
|
|
HD2
|
B:HIS402
|
3.0
|
11.7
|
1.0
|
|
CB
|
B:HIS447
|
3.1
|
10.4
|
1.0
|
|
HE1
|
B:HIS447
|
3.1
|
20.5
|
1.0
|
|
HE1
|
B:HIS402
|
3.2
|
11.7
|
1.0
|
|
HE2
|
B:PHE401
|
3.4
|
25.3
|
1.0
|
|
HA
|
B:HIS493
|
3.5
|
8.8
|
1.0
|
|
CE2
|
B:PHE401
|
3.5
|
13.1
|
1.0
|
|
CA
|
B:HIS447
|
3.5
|
9.1
|
1.0
|
|
HB3
|
B:HIS493
|
3.6
|
9.5
|
1.0
|
|
CZ
|
B:PHE401
|
3.7
|
14.8
|
1.0
|
|
HZ
|
B:PHE401
|
3.7
|
25.3
|
1.0
|
|
O
|
B:HOH1125
|
3.8
|
24.4
|
0.5
|
|
HG23
|
B:THR448
|
3.8
|
11.4
|
1.0
|
|
O
|
B:HIS493
|
3.9
|
10.9
|
1.0
|
|
CD2
|
B:HIS447
|
3.9
|
10.0
|
1.0
|
|
NE2
|
B:HIS447
|
4.0
|
9.7
|
1.0
|
|
CG
|
B:HIS402
|
4.0
|
9.7
|
1.0
|
|
HB2
|
B:HIS447
|
4.0
|
10.1
|
1.0
|
|
ND1
|
B:HIS402
|
4.1
|
12.8
|
1.0
|
|
CA
|
B:HIS493
|
4.1
|
8.2
|
1.0
|
|
CD2
|
B:PHE401
|
4.1
|
13.9
|
1.0
|
|
CB
|
B:HIS493
|
4.1
|
9.2
|
1.0
|
|
C
|
B:HIS447
|
4.1
|
9.5
|
1.0
|
|
H
|
B:THR448
|
4.1
|
10.1
|
1.0
|
|
N
|
B:THR448
|
4.3
|
9.7
|
1.0
|
|
CG
|
B:HIS493
|
4.3
|
8.7
|
1.0
|
|
C
|
B:HIS493
|
4.3
|
8.6
|
1.0
|
|
HD2
|
B:PHE401
|
4.3
|
25.3
|
1.0
|
|
CE1
|
B:PHE401
|
4.4
|
26.1
|
1.0
|
|
O
|
B:MET446
|
4.6
|
9.3
|
1.0
|
|
CD2
|
B:HIS493
|
4.6
|
9.3
|
1.0
|
|
O
|
B:HOH855
|
4.6
|
23.8
|
0.5
|
|
N
|
B:HIS447
|
4.7
|
8.7
|
1.0
|
|
HD2
|
B:HIS493
|
4.7
|
10.4
|
1.0
|
|
CG2
|
B:THR448
|
4.7
|
11.5
|
1.0
|
|
HE2
|
B:HIS447
|
4.8
|
9.3
|
0.0
|
|
HD2
|
B:HIS447
|
4.8
|
20.5
|
1.0
|
|
CG
|
B:PHE401
|
4.8
|
11.8
|
1.0
|
|
HE1
|
B:HIS101
|
4.8
|
10.5
|
1.0
|
|
ND1
|
B:HIS493
|
4.8
|
11.3
|
1.0
|
|
HD1
|
B:HIS402
|
4.9
|
11.8
|
0.0
|
|
HG21
|
B:THR448
|
4.9
|
11.4
|
1.0
|
|
O
|
B:HIS447
|
4.9
|
10.3
|
1.0
|
|
HE1
|
B:PHE401
|
4.9
|
25.3
|
1.0
|
|
O
|
B:HOH1205
|
4.9
|
24.1
|
0.5
|
|
CD1
|
B:PHE401
|
4.9
|
23.3
|
1.0
|
|
HA
|
B:THR448
|
5.0
|
11.4
|
1.0
|
|
Reference:
L.A.Varfolomeeva,
K.M.Polyakov,
N.S.Shipkov,
N.I.Dergousova,
K.M.Boyko,
T.V.Tikhonova,
V.O.Popov.
Structure of Thiocyanate Dehydrogenase From Pelomicrobium Methylotrophicum at Atomic Resolution To Be Published.
Page generated: Wed Jul 31 10:08:03 2024
|
