Copper in PDB 2fqf: Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
Protein crystallography data
The structure of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations, PDB code: 2fqf
was solved by
X.Li,
Z.Wei,
M.Zhang,
M.Teng,
W.Gong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.00
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
69.426,
73.252,
189.885,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.7 /
23.3
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
(pdb code 2fqf). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations, PDB code: 2fqf:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2fqf
Go back to
Copper Binding Sites List in 2fqf
Copper binding site 1 out
of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:23.6
occ:1.00
|
ND1
|
A:HIS443
|
2.0
|
19.9
|
1.0
|
ND1
|
A:HIS505
|
2.1
|
18.2
|
1.0
|
SG
|
A:CYS500
|
2.2
|
19.1
|
1.0
|
CE1
|
A:HIS443
|
2.9
|
21.7
|
1.0
|
CG
|
A:HIS505
|
3.0
|
19.6
|
1.0
|
CG
|
A:HIS443
|
3.1
|
19.8
|
1.0
|
CE1
|
A:HIS505
|
3.1
|
18.3
|
1.0
|
CB
|
A:CYS500
|
3.1
|
18.1
|
1.0
|
SD
|
A:MET510
|
3.2
|
23.2
|
1.0
|
CB
|
A:HIS505
|
3.3
|
20.1
|
1.0
|
CB
|
A:HIS443
|
3.5
|
18.7
|
1.0
|
O
|
A:LEU442
|
3.6
|
20.7
|
1.0
|
CA
|
A:HIS443
|
3.7
|
19.0
|
1.0
|
CE
|
A:MET510
|
3.9
|
23.7
|
1.0
|
CB
|
A:LEU502
|
4.0
|
17.2
|
1.0
|
NE2
|
A:HIS443
|
4.1
|
22.5
|
1.0
|
CD2
|
A:HIS505
|
4.2
|
19.3
|
1.0
|
CD2
|
A:HIS443
|
4.2
|
20.6
|
1.0
|
NE2
|
A:HIS505
|
4.2
|
18.1
|
1.0
|
C
|
A:LEU442
|
4.4
|
21.1
|
1.0
|
N
|
A:HIS443
|
4.5
|
19.9
|
1.0
|
CA
|
A:CYS500
|
4.6
|
18.3
|
1.0
|
CD1
|
A:LEU502
|
4.6
|
17.7
|
1.0
|
CG
|
A:MET510
|
4.8
|
21.3
|
1.0
|
CG
|
A:LEU502
|
4.8
|
18.3
|
1.0
|
CA
|
A:HIS505
|
4.8
|
20.3
|
1.0
|
O
|
A:LEU502
|
4.9
|
17.0
|
1.0
|
C
|
A:HIS443
|
4.9
|
18.3
|
1.0
|
N
|
A:LEU502
|
4.9
|
17.7
|
1.0
|
|
Copper binding site 2 out
of 4 in 2fqf
Go back to
Copper Binding Sites List in 2fqf
Copper binding site 2 out
of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:19.7
occ:0.30
|
NE2
|
A:HIS101
|
1.9
|
24.1
|
1.0
|
NE2
|
A:HIS446
|
1.9
|
16.4
|
1.0
|
O
|
A:HOH777
|
2.6
|
22.1
|
1.0
|
CE1
|
A:HIS101
|
2.7
|
22.9
|
1.0
|
CD2
|
A:HIS446
|
2.8
|
16.2
|
1.0
|
CE1
|
A:HIS446
|
2.9
|
16.6
|
1.0
|
CD2
|
A:HIS101
|
3.0
|
23.4
|
1.0
|
CD2
|
A:HIS448
|
3.2
|
19.2
|
1.0
|
NE2
|
A:HIS448
|
3.3
|
20.0
|
1.0
|
CA
|
A:HIS103
|
3.4
|
16.9
|
1.0
|
CG
|
A:HIS103
|
3.5
|
18.0
|
1.0
|
ND1
|
A:HIS103
|
3.5
|
18.3
|
1.0
|
O1
|
A:C2O602
|
3.6
|
25.4
|
0.8
|
CU2
|
A:C2O602
|
3.6
|
25.8
|
0.4
|
CB
|
A:HIS103
|
3.6
|
16.9
|
1.0
|
CG
|
A:HIS448
|
3.8
|
19.1
|
1.0
|
ND1
|
A:HIS101
|
3.9
|
23.2
|
1.0
|
CG
|
A:HIS446
|
4.0
|
16.7
|
1.0
|
CE1
|
A:HIS448
|
4.0
|
19.5
|
1.0
|
ND1
|
A:HIS446
|
4.0
|
17.9
|
1.0
|
CG
|
A:HIS101
|
4.1
|
22.9
|
1.0
|
CU3
|
A:C2O602
|
4.1
|
23.5
|
0.8
|
CE1
|
A:HIS103
|
4.2
|
17.2
|
1.0
|
CD2
|
A:HIS103
|
4.2
|
16.0
|
1.0
|
N
|
A:GLY104
|
4.2
|
17.0
|
1.0
|
ND1
|
A:HIS448
|
4.3
|
19.8
|
1.0
|
N
|
A:HIS103
|
4.3
|
17.5
|
1.0
|
C
|
A:HIS103
|
4.3
|
16.6
|
1.0
|
CA
|
A:HIS448
|
4.5
|
18.1
|
1.0
|
NE2
|
A:HIS103
|
4.5
|
19.9
|
1.0
|
O
|
A:HOH772
|
4.6
|
23.2
|
1.0
|
O
|
A:HOH724
|
4.6
|
16.0
|
1.0
|
CB
|
A:HIS448
|
4.7
|
17.9
|
1.0
|
O
|
A:TRP102
|
4.7
|
18.8
|
1.0
|
C
|
A:TRP102
|
4.8
|
18.3
|
1.0
|
N
|
A:HIS448
|
5.0
|
18.1
|
1.0
|
|
Copper binding site 3 out
of 4 in 2fqf
Go back to
Copper Binding Sites List in 2fqf
Copper binding site 3 out
of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:25.8
occ:0.40
|
CU2
|
A:C2O602
|
0.0
|
25.8
|
0.4
|
NE2
|
A:HIS448
|
2.0
|
20.0
|
1.0
|
NE2
|
A:HIS499
|
2.1
|
18.0
|
1.0
|
O1
|
A:C2O602
|
2.1
|
25.4
|
0.8
|
NE2
|
A:HIS143
|
2.2
|
29.7
|
1.0
|
CE1
|
A:HIS499
|
2.9
|
18.1
|
1.0
|
CE1
|
A:HIS448
|
2.9
|
19.5
|
1.0
|
CD2
|
A:HIS143
|
3.0
|
27.7
|
1.0
|
CD2
|
A:HIS448
|
3.1
|
19.2
|
1.0
|
CD2
|
A:HIS499
|
3.2
|
18.2
|
1.0
|
CE1
|
A:HIS143
|
3.3
|
29.0
|
1.0
|
NE2
|
A:HIS101
|
3.5
|
24.1
|
1.0
|
CD2
|
A:HIS446
|
3.5
|
16.2
|
1.0
|
CU
|
A:CU603
|
3.6
|
19.7
|
0.3
|
CD2
|
A:HIS101
|
3.6
|
23.4
|
1.0
|
O
|
A:HOH971
|
3.7
|
40.7
|
1.0
|
NE2
|
A:HIS446
|
4.1
|
16.4
|
1.0
|
ND1
|
A:HIS448
|
4.1
|
19.8
|
1.0
|
ND1
|
A:HIS499
|
4.1
|
17.0
|
1.0
|
CG
|
A:HIS448
|
4.2
|
19.1
|
1.0
|
CG
|
A:HIS143
|
4.2
|
25.2
|
1.0
|
CG
|
A:HIS499
|
4.2
|
17.1
|
1.0
|
CU3
|
A:C2O602
|
4.3
|
23.5
|
0.8
|
ND1
|
A:HIS143
|
4.3
|
28.8
|
1.0
|
CE1
|
A:HIS101
|
4.3
|
22.9
|
1.0
|
CG
|
A:HIS101
|
4.4
|
22.9
|
1.0
|
CE1
|
A:HIS141
|
4.6
|
19.7
|
1.0
|
CG
|
A:HIS446
|
4.8
|
16.7
|
1.0
|
CD2
|
A:HIS501
|
4.8
|
18.5
|
1.0
|
ND1
|
A:HIS101
|
4.8
|
23.2
|
1.0
|
CB
|
A:MET497
|
4.9
|
20.0
|
1.0
|
NE2
|
A:HIS141
|
4.9
|
19.5
|
1.0
|
NE2
|
A:HIS501
|
4.9
|
18.1
|
1.0
|
|
Copper binding site 4 out
of 4 in 2fqf
Go back to
Copper Binding Sites List in 2fqf
Copper binding site 4 out
of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:23.5
occ:0.80
|
CU3
|
A:C2O602
|
0.0
|
23.5
|
0.8
|
ND1
|
A:HIS103
|
2.0
|
18.3
|
1.0
|
NE2
|
A:HIS141
|
2.0
|
19.5
|
1.0
|
NE2
|
A:HIS501
|
2.2
|
18.1
|
1.0
|
O1
|
A:C2O602
|
2.3
|
25.4
|
0.8
|
CE1
|
A:HIS103
|
2.9
|
17.2
|
1.0
|
CE1
|
A:HIS141
|
3.0
|
19.7
|
1.0
|
CG
|
A:HIS103
|
3.0
|
18.0
|
1.0
|
CD2
|
A:HIS141
|
3.0
|
18.6
|
1.0
|
CD2
|
A:HIS501
|
3.1
|
18.5
|
1.0
|
CE1
|
A:HIS501
|
3.2
|
19.2
|
1.0
|
CB
|
A:HIS103
|
3.4
|
16.9
|
1.0
|
CZ2
|
A:TRP139
|
3.7
|
15.4
|
1.0
|
CD2
|
A:HIS101
|
4.0
|
23.4
|
1.0
|
NE2
|
A:HIS103
|
4.1
|
19.9
|
1.0
|
ND1
|
A:HIS141
|
4.1
|
19.2
|
1.0
|
CE2
|
A:TRP139
|
4.1
|
14.0
|
1.0
|
CD2
|
A:HIS103
|
4.1
|
16.0
|
1.0
|
CG
|
A:HIS141
|
4.1
|
18.7
|
1.0
|
CU
|
A:CU603
|
4.1
|
19.7
|
0.3
|
NE1
|
A:TRP139
|
4.1
|
12.4
|
1.0
|
CG
|
A:HIS501
|
4.2
|
17.7
|
1.0
|
CD2
|
A:HIS446
|
4.3
|
16.2
|
1.0
|
ND1
|
A:HIS501
|
4.3
|
18.4
|
1.0
|
CU2
|
A:C2O602
|
4.3
|
25.8
|
0.4
|
O
|
A:HOH971
|
4.3
|
40.7
|
1.0
|
NE2
|
A:HIS101
|
4.3
|
24.1
|
1.0
|
NE2
|
A:HIS446
|
4.4
|
16.4
|
1.0
|
CH2
|
A:TRP139
|
4.5
|
15.3
|
1.0
|
CA
|
A:HIS103
|
4.7
|
16.9
|
1.0
|
|
Reference:
X.Li,
Z.Wei,
M.Zhang,
X.Peng,
G.Yu,
M.Teng,
W.Gong.
Crystal Structures of E. Coli Laccase Cueo at Different Copper Concentrations. Biochem.Biophys.Res.Commun. V. 354 21 2007.
ISSN: ISSN 0006-291X
PubMed: 17217912
DOI: 10.1016/J.BBRC.2006.12.116
Page generated: Tue Jul 30 23:34:38 2024
|