Copper in PDB 2h5u: Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
Enzymatic activity of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
All present enzymatic activity of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution:
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution, PDB code: 2h5u
was solved by
A.V.Lyashenko,
A.G.Gabdoulkhakov,
V.N.Zaitsev,
V.S.Lamzin,
P.F.Lindley,
I.Bento,
C.Betzel,
N.E.Zhukhlistova,
Y.N.Zhukova,
A.M.Mikhailov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.27 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
52.581,
77.101,
130.884,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19 /
23.8
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
(pdb code 2h5u). 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 Structure of Laccase From Cerrena Maxima at 1.9A Resolution, PDB code: 2h5u:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2h5u
Go back to
Copper Binding Sites List in 2h5u
Copper binding site 1 out
of 4 in the Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:12.9
occ:0.30
|
ND1
|
A:HIS458
|
2.0
|
12.6
|
1.0
|
ND1
|
A:HIS395
|
2.0
|
14.9
|
1.0
|
SG
|
A:CYS453
|
2.3
|
11.5
|
1.0
|
CE1
|
A:HIS395
|
2.7
|
16.2
|
1.0
|
CE1
|
A:HIS458
|
2.9
|
11.8
|
1.0
|
CG
|
A:HIS458
|
3.0
|
12.0
|
1.0
|
CG
|
A:HIS395
|
3.1
|
14.6
|
1.0
|
CB
|
A:HIS458
|
3.4
|
11.9
|
1.0
|
CB
|
A:CYS453
|
3.6
|
9.8
|
1.0
|
CD1
|
A:ILE455
|
3.6
|
10.7
|
1.0
|
CB
|
A:HIS395
|
3.7
|
13.8
|
1.0
|
CD2
|
A:PHE463
|
3.7
|
9.6
|
1.0
|
CE2
|
A:PHE463
|
3.9
|
10.3
|
1.0
|
NE2
|
A:HIS395
|
3.9
|
16.2
|
1.0
|
CB
|
A:ILE455
|
4.0
|
10.7
|
1.0
|
NE2
|
A:HIS458
|
4.1
|
12.2
|
1.0
|
CD2
|
A:HIS395
|
4.1
|
15.3
|
1.0
|
CD2
|
A:HIS458
|
4.1
|
11.8
|
1.0
|
CG1
|
A:ILE455
|
4.2
|
10.7
|
1.0
|
CA
|
A:HIS395
|
4.2
|
13.8
|
1.0
|
O
|
A:GLY392
|
4.5
|
19.8
|
1.0
|
CG2
|
A:ILE455
|
4.7
|
10.6
|
1.0
|
CD
|
A:PRO396
|
4.9
|
11.9
|
1.0
|
CA
|
A:HIS458
|
4.9
|
11.9
|
1.0
|
CZ
|
A:PHE337
|
4.9
|
10.7
|
1.0
|
CA
|
A:CYS453
|
4.9
|
9.8
|
1.0
|
|
Copper binding site 2 out
of 4 in 2h5u
Go back to
Copper Binding Sites List in 2h5u
Copper binding site 2 out
of 4 in the Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:11.8
occ:1.00
|
ND1
|
A:HIS66
|
2.0
|
7.5
|
1.0
|
NE2
|
A:HIS454
|
2.0
|
10.1
|
1.0
|
NE2
|
A:HIS109
|
2.0
|
6.7
|
1.0
|
CE1
|
A:HIS454
|
2.8
|
8.9
|
1.0
|
CE1
|
A:HIS66
|
2.8
|
7.2
|
1.0
|
CE1
|
A:HIS109
|
2.9
|
6.0
|
1.0
|
O
|
A:HOH1132
|
3.0
|
22.6
|
1.0
|
CD2
|
A:HIS109
|
3.1
|
5.3
|
1.0
|
CG
|
A:HIS66
|
3.1
|
6.7
|
1.0
|
CD2
|
A:HIS454
|
3.1
|
9.6
|
1.0
|
CZ2
|
A:TRP107
|
3.6
|
4.1
|
1.0
|
CB
|
A:HIS66
|
3.6
|
6.4
|
1.0
|
CD2
|
A:HIS64
|
3.7
|
6.1
|
1.0
|
CE2
|
A:TRP107
|
3.9
|
4.2
|
1.0
|
ND1
|
A:HIS454
|
4.0
|
9.2
|
1.0
|
ND1
|
A:HIS109
|
4.0
|
5.3
|
1.0
|
NE2
|
A:HIS66
|
4.0
|
6.2
|
1.0
|
NE1
|
A:TRP107
|
4.1
|
3.9
|
1.0
|
CU
|
A:CU604
|
4.1
|
8.6
|
0.5
|
CG
|
A:HIS109
|
4.1
|
5.5
|
1.0
|
CD2
|
A:HIS66
|
4.2
|
6.2
|
1.0
|
CG
|
A:HIS454
|
4.2
|
9.7
|
1.0
|
NE2
|
A:HIS64
|
4.2
|
6.4
|
1.0
|
CH2
|
A:TRP107
|
4.3
|
4.3
|
1.0
|
CD2
|
A:HIS398
|
4.4
|
7.6
|
1.0
|
CB
|
A:ALA241
|
4.4
|
5.6
|
1.0
|
O
|
A:HOH1109
|
4.4
|
18.9
|
0.8
|
NE2
|
A:HIS398
|
4.6
|
8.1
|
1.0
|
CA
|
A:HIS66
|
4.7
|
6.2
|
1.0
|
CU
|
A:CU603
|
4.8
|
12.7
|
1.0
|
CD2
|
A:TRP107
|
4.9
|
3.8
|
1.0
|
CG
|
A:HIS64
|
4.9
|
6.9
|
1.0
|
|
Copper binding site 3 out
of 4 in 2h5u
Go back to
Copper Binding Sites List in 2h5u
Copper binding site 3 out
of 4 in the Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:12.7
occ:1.00
|
O
|
A:HOH1132
|
1.8
|
22.6
|
1.0
|
NE2
|
A:HIS400
|
2.0
|
8.4
|
1.0
|
NE2
|
A:HIS452
|
2.0
|
9.8
|
1.0
|
NE2
|
A:HIS111
|
2.0
|
7.9
|
1.0
|
CE1
|
A:HIS400
|
2.7
|
7.4
|
1.0
|
CE1
|
A:HIS111
|
2.9
|
7.2
|
1.0
|
CD2
|
A:HIS452
|
3.0
|
9.3
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
9.4
|
1.0
|
CD2
|
A:HIS111
|
3.0
|
6.8
|
1.0
|
CD2
|
A:HIS400
|
3.2
|
7.0
|
1.0
|
O
|
A:HOH1109
|
3.7
|
18.9
|
0.8
|
ND1
|
A:HIS400
|
3.9
|
6.8
|
1.0
|
CD2
|
A:HIS398
|
4.0
|
7.6
|
1.0
|
ND1
|
A:HIS452
|
4.1
|
9.5
|
1.0
|
ND1
|
A:HIS111
|
4.1
|
6.9
|
1.0
|
CG
|
A:HIS452
|
4.1
|
8.8
|
1.0
|
CG
|
A:HIS111
|
4.1
|
6.6
|
1.0
|
CG
|
A:HIS400
|
4.2
|
7.3
|
1.0
|
CD2
|
A:PHE450
|
4.3
|
6.7
|
1.0
|
CU
|
A:CU604
|
4.4
|
8.6
|
0.5
|
CD2
|
A:HIS64
|
4.5
|
6.1
|
1.0
|
NE2
|
A:HIS454
|
4.6
|
10.1
|
1.0
|
CB
|
A:PHE450
|
4.6
|
7.1
|
1.0
|
CD2
|
A:HIS454
|
4.7
|
9.6
|
1.0
|
NE2
|
A:HIS64
|
4.7
|
6.4
|
1.0
|
CG
|
A:PRO79
|
4.7
|
7.2
|
1.0
|
NE2
|
A:HIS398
|
4.8
|
8.1
|
1.0
|
CU
|
A:CU602
|
4.8
|
11.8
|
1.0
|
CG
|
A:PHE450
|
4.9
|
6.8
|
1.0
|
CE1
|
A:HIS109
|
4.9
|
6.0
|
1.0
|
|
Copper binding site 4 out
of 4 in 2h5u
Go back to
Copper Binding Sites List in 2h5u
Copper binding site 4 out
of 4 in the Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structure of Laccase From Cerrena Maxima at 1.9A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:8.6
occ:0.50
|
NE2
|
A:HIS398
|
2.0
|
8.1
|
1.0
|
NE2
|
A:HIS64
|
2.0
|
6.4
|
1.0
|
O
|
A:HOH607
|
2.6
|
4.8
|
1.0
|
CD2
|
A:HIS398
|
2.8
|
7.6
|
1.0
|
CE1
|
A:HIS64
|
2.9
|
6.4
|
1.0
|
CD2
|
A:HIS64
|
3.0
|
6.1
|
1.0
|
CE1
|
A:HIS398
|
3.1
|
7.8
|
1.0
|
NE2
|
A:HIS400
|
3.4
|
8.4
|
1.0
|
CE1
|
A:HIS400
|
3.4
|
7.4
|
1.0
|
ND1
|
A:HIS66
|
3.5
|
7.5
|
1.0
|
ND1
|
A:HIS400
|
3.6
|
6.8
|
1.0
|
CD2
|
A:HIS400
|
3.6
|
7.0
|
1.0
|
CG
|
A:HIS66
|
3.6
|
6.7
|
1.0
|
O
|
A:HOH1132
|
3.7
|
22.6
|
1.0
|
CG
|
A:HIS400
|
3.7
|
7.3
|
1.0
|
CE1
|
A:HIS66
|
3.8
|
7.2
|
1.0
|
CA
|
A:HIS66
|
3.9
|
6.2
|
1.0
|
ND1
|
A:HIS64
|
4.0
|
6.4
|
1.0
|
CG
|
A:HIS398
|
4.0
|
8.1
|
1.0
|
CD2
|
A:HIS66
|
4.0
|
6.2
|
1.0
|
N
|
A:GLY67
|
4.0
|
6.1
|
1.0
|
NE2
|
A:HIS66
|
4.1
|
6.2
|
1.0
|
ND1
|
A:HIS398
|
4.1
|
8.3
|
1.0
|
CU
|
A:CU602
|
4.1
|
11.8
|
1.0
|
CG
|
A:HIS64
|
4.1
|
6.9
|
1.0
|
CB
|
A:HIS66
|
4.1
|
6.4
|
1.0
|
CU
|
A:CU603
|
4.4
|
12.7
|
1.0
|
C
|
A:HIS66
|
4.5
|
6.3
|
1.0
|
O
|
A:HOH632
|
4.5
|
10.9
|
1.0
|
CA
|
A:HIS400
|
4.5
|
7.4
|
1.0
|
CB
|
A:HIS400
|
4.6
|
7.3
|
1.0
|
O
|
A:HOH724
|
4.7
|
13.8
|
1.0
|
N
|
A:HIS66
|
4.9
|
6.2
|
1.0
|
|
Reference:
A.V.Lyashenko,
N.E.Zhukhlistova,
A.G.Gabdoulkhakov,
V.N.Zaitsev,
I.Bento,
V.S.Lamzin,
C.Betzel,
P.F.Lindley,
O.V.Koroleva,
Y.N.Zhukova,
E.V.Stepanova,
E.Y.Morgunova,
W.Voelter,
K.Schirwitz,
V.I.Tishkov,
G.S.Kachalova,
E.A.Cherkashyn,
A.M.Mikhailov.
Purification, Crystallization and Preliminary X-Ray Study of the Fungal Laccase From Cerrena Maxima Acta Crystallogr.,Sect.F V. 62 954 2006.
ISSN: ESSN 1744-3091
PubMed: 17012782
DOI: 10.1107/S1744309106036578
Page generated: Tue Jul 30 23:39:32 2024
|