Atomistry » Copper » PDB 5wbd-5z85 » 5z1x
Atomistry »
  Copper »
    PDB 5wbd-5z85 »
      5z1x »

Copper in PDB 5z1x: Crystal Structure of Laccase From Cerrena Sp. RSD1

Enzymatic activity of Crystal Structure of Laccase From Cerrena Sp. RSD1

All present enzymatic activity of Crystal Structure of Laccase From Cerrena Sp. RSD1:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of Laccase From Cerrena Sp. RSD1, PDB code: 5z1x was solved by C.C.Lee, M.H.Wu, T.H.Ho, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.626, 88.795, 147.815, 90.00, 90.00, 90.00
R / Rfree (%) 12.6 / 14.9

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Laccase From Cerrena Sp. RSD1 (pdb code 5z1x). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the Crystal Structure of Laccase From Cerrena Sp. RSD1, PDB code: 5z1x:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Copper binding site 1 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 1 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


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 Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu509

b:12.3
occ:1.00
ND1 A:HIS454 2.1 12.0 1.0
ND1 A:HIS393 2.1 11.8 1.0
SG A:CYS449 2.2 11.6 1.0
CE1 A:HIS393 3.0 12.6 1.0
CE1 A:HIS454 3.0 12.3 1.0
CG A:HIS454 3.1 11.7 1.0
CG A:HIS393 3.2 11.2 1.0
CB A:CYS449 3.3 11.3 1.0
CB A:HIS454 3.4 11.4 1.0
CD1 A:ILE451 3.5 12.5 1.0
CB A:HIS393 3.5 10.9 1.0
CD2 A:PHE459 3.7 11.6 1.0
CB A:ILE451 3.7 11.5 1.0
CE2 A:PHE459 3.9 12.1 1.0
CG1 A:ILE451 4.0 12.1 1.0
CA A:HIS393 4.0 10.6 1.0
NE2 A:HIS393 4.1 12.3 1.0
NE2 A:HIS454 4.1 13.0 1.0
CD2 A:HIS454 4.2 12.7 1.0
CD2 A:HIS393 4.2 11.5 1.0
CG2 A:ILE451 4.5 11.9 1.0
CA A:CYS449 4.6 10.9 1.0
O A:GLY390 4.7 16.6 1.0
N A:ILE451 4.7 11.2 1.0
CD A:PRO394 4.7 10.5 1.0
CA A:ILE451 4.8 11.5 1.0
O A:ILE451 4.8 12.2 1.0
CA A:HIS454 4.9 11.8 1.0
CG A:PHE459 5.0 11.3 1.0
C A:HIS393 5.0 10.6 1.0

Copper binding site 2 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 2 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


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 Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu510

b:13.9
occ:1.00
NE2 A:HIS396 1.9 10.1 1.0
NE2 A:HIS64 2.0 10.7 1.0
O A:HOH964 2.5 13.2 1.0
O2 A:OXY513 2.8 26.4 1.0
CE1 A:HIS64 2.9 10.9 1.0
CD2 A:HIS396 2.9 11.0 1.0
CE1 A:HIS396 2.9 10.7 1.0
CD2 A:HIS64 3.0 11.2 1.0
NE2 A:HIS398 3.4 11.1 1.0
CE1 A:HIS398 3.5 10.5 1.0
ND1 A:HIS66 3.5 10.4 1.0
CD2 A:HIS398 3.6 11.1 1.0
O1 A:OXY513 3.7 22.8 1.0
CG A:HIS66 3.7 10.0 1.0
ND1 A:HIS398 3.7 10.6 1.0
CG A:HIS398 3.8 10.6 1.0
CA A:HIS66 3.9 9.8 1.0
CE1 A:HIS66 3.9 10.8 1.0
ND1 A:HIS64 4.0 10.7 1.0
ND1 A:HIS396 4.0 10.6 1.0
CG A:HIS396 4.0 10.8 1.0
N A:GLY67 4.0 10.1 1.0
CU A:CU511 4.1 13.6 1.0
CG A:HIS64 4.1 10.6 1.0
CB A:HIS66 4.1 9.7 1.0
CD2 A:HIS66 4.2 9.7 1.0
NE2 A:HIS66 4.3 10.3 1.0
CU A:CU512 4.3 17.6 1.0
C A:HIS66 4.5 10.0 1.0
O A:HOH763 4.5 13.8 1.0
O A:HOH700 4.6 12.3 1.0
CA A:HIS398 4.6 10.4 1.0
CB A:HIS398 4.7 10.9 1.0
N A:HIS66 4.9 9.7 1.0

Copper binding site 3 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 3 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


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 Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu511

b:13.6
occ:1.00
ND1 A:HIS66 2.0 10.4 1.0
NE2 A:HIS109 2.0 11.2 1.0
NE2 A:HIS450 2.2 11.2 1.0
O2 A:OXY513 2.4 26.4 1.0
CE1 A:HIS66 2.9 10.8 1.0
CD2 A:HIS109 3.0 10.8 1.0
CE1 A:HIS450 3.0 11.7 1.0
CE1 A:HIS109 3.0 10.8 1.0
CG A:HIS66 3.0 10.0 1.0
O1 A:OXY513 3.3 22.8 1.0
CD2 A:HIS450 3.3 11.2 1.0
CZ2 A:TRP107 3.4 9.8 1.0
CB A:HIS66 3.4 9.7 1.0
CE2 A:TRP107 3.7 9.8 1.0
CD2 A:HIS64 3.9 11.2 1.0
NE1 A:TRP107 3.9 10.2 1.0
NE2 A:HIS66 4.1 10.3 1.0
CU A:CU510 4.1 13.9 1.0
ND1 A:HIS109 4.1 10.7 1.0
CD2 A:HIS66 4.1 9.7 1.0
CG A:HIS109 4.1 10.6 1.0
CH2 A:TRP107 4.2 9.8 1.0
ND1 A:HIS450 4.2 11.5 1.0
NE2 A:HIS64 4.3 10.7 1.0
CG A:HIS450 4.4 11.5 1.0
CD2 A:HIS396 4.4 11.0 1.0
NE2 A:HIS396 4.4 10.1 1.0
O A:HOH1116 4.5 18.8 1.0
CA A:HIS66 4.6 9.8 1.0
CD2 A:TRP107 4.7 9.6 1.0
CD1 A:TRP107 4.9 9.7 1.0
CU A:CU512 4.9 17.6 1.0

Copper binding site 4 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 4 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


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 Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu512

b:17.6
occ:1.00
O1 A:OXY513 1.7 22.8 1.0
NE2 A:HIS448 2.0 12.5 1.0
NE2 A:HIS398 2.0 11.1 1.0
NE2 A:HIS111 2.1 10.7 1.0
O2 A:OXY513 2.7 26.4 1.0
CE1 A:HIS398 2.9 10.5 1.0
CE1 A:HIS448 3.0 12.7 1.0
CD2 A:HIS448 3.0 12.5 1.0
CE1 A:HIS111 3.0 11.5 1.0
CD2 A:HIS111 3.1 10.6 1.0
CD2 A:HIS398 3.2 11.1 1.0
O A:HOH1116 3.6 18.8 1.0
CD2 A:HIS396 3.9 11.0 1.0
ND1 A:HIS398 4.0 10.6 1.0
ND1 A:HIS448 4.1 12.3 1.0
CG A:HIS448 4.1 11.8 1.0
ND1 A:HIS111 4.2 11.3 1.0
CG A:HIS398 4.2 10.6 1.0
CG A:HIS111 4.2 10.9 1.0
CU A:CU510 4.3 13.9 1.0
CD2 A:PHE446 4.4 13.0 1.0
CD2 A:HIS64 4.4 11.2 1.0
NE2 A:HIS396 4.6 10.1 1.0
CB A:PHE446 4.6 12.0 1.0
NE2 A:HIS64 4.6 10.7 1.0
CE1 A:HIS109 4.8 10.8 1.0
CG A:PRO79 4.8 11.1 1.0
NE2 A:HIS450 4.9 11.2 1.0
CU A:CU511 4.9 13.6 1.0
CG A:PHE446 5.0 11.9 1.0

Copper binding site 5 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 5 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Laccase From Cerrena Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu509

b:12.9
occ:1.00
ND1 B:HIS454 2.1 13.1 1.0
ND1 B:HIS393 2.1 12.5 1.0
SG B:CYS449 2.2 12.3 1.0
CE1 B:HIS393 3.0 13.0 1.0
CE1 B:HIS454 3.0 13.3 1.0
CG B:HIS454 3.1 12.0 1.0
CG B:HIS393 3.2 12.4 1.0
CB B:CYS449 3.3 11.6 1.0
CB B:HIS454 3.4 12.2 1.0
CD1 B:ILE451 3.5 12.6 1.0
CB B:HIS393 3.5 12.3 1.0
CD2 B:PHE459 3.7 12.9 1.0
CB B:ILE451 3.7 12.2 1.0
CE2 B:PHE459 3.9 13.2 1.0
CG1 B:ILE451 4.0 12.6 1.0
CA B:HIS393 4.0 12.0 1.0
NE2 B:HIS393 4.1 14.0 1.0
NE2 B:HIS454 4.1 13.3 1.0
CD2 B:HIS454 4.2 12.7 1.0
CD2 B:HIS393 4.2 13.3 1.0
CG2 B:ILE451 4.5 12.2 1.0
CA B:CYS449 4.6 11.3 1.0
CD B:PRO394 4.7 11.3 1.0
N B:ILE451 4.7 11.5 1.0
O B:GLY390 4.8 16.9 1.0
CA B:ILE451 4.8 12.0 1.0
O B:ILE451 4.8 11.8 1.0
CA B:HIS454 4.9 12.3 1.0
CG B:PHE459 5.0 13.0 1.0
C B:HIS393 5.0 12.0 1.0

Copper binding site 6 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 6 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Laccase From Cerrena Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu510

b:15.2
occ:1.00
NE2 B:HIS396 1.9 12.0 1.0
NE2 B:HIS64 1.9 11.2 1.0
O B:HOH917 2.5 13.9 1.0
CE1 B:HIS64 2.9 11.5 1.0
CD2 B:HIS396 2.9 12.1 1.0
CE1 B:HIS396 2.9 11.8 1.0
CD2 B:HIS64 3.0 11.8 1.0
O2 B:OXY513 3.0 61.9 1.0
NE2 B:HIS398 3.4 11.8 1.0
ND1 B:HIS66 3.5 10.6 1.0
CE1 B:HIS398 3.5 11.3 1.0
CD2 B:HIS398 3.6 11.7 1.0
CG B:HIS66 3.7 10.8 1.0
ND1 B:HIS398 3.7 11.8 1.0
O1 B:OXY513 3.8 45.5 1.0
CG B:HIS398 3.8 11.5 1.0
CA B:HIS66 3.9 11.1 1.0
CE1 B:HIS66 3.9 10.8 1.0
ND1 B:HIS64 4.0 11.8 1.0
ND1 B:HIS396 4.0 11.8 1.0
CG B:HIS396 4.0 11.8 1.0
CG B:HIS64 4.0 11.3 1.0
N B:GLY67 4.1 11.8 1.0
CU B:CU511 4.1 14.5 1.0
CB B:HIS66 4.1 10.8 1.0
CD2 B:HIS66 4.2 11.3 1.0
NE2 B:HIS66 4.3 11.6 1.0
CU B:CU512 4.3 19.3 1.0
C B:HIS66 4.5 11.1 1.0
O B:HOH765 4.5 14.8 1.0
O B:HOH696 4.6 13.7 1.0
CA B:HIS398 4.6 11.4 1.0
CB B:HIS398 4.7 11.5 1.0
N B:HIS66 4.9 10.7 1.0

Copper binding site 7 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 7 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of Laccase From Cerrena Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu511

b:14.5
occ:1.00
ND1 B:HIS66 2.0 10.6 1.0
O2 B:OXY513 2.0 61.9 1.0
NE2 B:HIS109 2.1 11.5 1.0
NE2 B:HIS450 2.2 11.8 1.0
CE1 B:HIS66 2.9 10.8 1.0
CD2 B:HIS109 3.0 11.2 1.0
CE1 B:HIS450 3.0 11.6 1.0
CG B:HIS66 3.0 10.8 1.0
O1 B:OXY513 3.1 45.5 1.0
CE1 B:HIS109 3.1 11.0 1.0
CD2 B:HIS450 3.3 11.7 1.0
CB B:HIS66 3.4 10.8 1.0
CZ2 B:TRP107 3.4 10.1 1.0
CE2 B:TRP107 3.7 9.7 1.0
CD2 B:HIS64 3.9 11.8 1.0
NE1 B:TRP107 3.9 10.3 1.0
NE2 B:HIS66 4.1 11.6 1.0
CU B:CU510 4.1 15.2 1.0
CD2 B:HIS66 4.1 11.3 1.0
ND1 B:HIS109 4.1 11.4 1.0
CG B:HIS109 4.1 10.7 1.0
CH2 B:TRP107 4.2 10.9 1.0
ND1 B:HIS450 4.2 11.6 1.0
NE2 B:HIS64 4.3 11.2 1.0
CG B:HIS450 4.4 11.7 1.0
CD2 B:HIS396 4.5 12.1 1.0
NE2 B:HIS396 4.5 12.0 1.0
O B:HOH1026 4.6 19.1 1.0
CA B:HIS66 4.6 11.1 1.0
CD2 B:TRP107 4.7 10.0 1.0
CD1 B:TRP107 4.9 9.9 1.0
CU B:CU512 4.9 19.3 1.0

Copper binding site 8 out of 8 in 5z1x

Go back to Copper Binding Sites List in 5z1x
Copper binding site 8 out of 8 in the Crystal Structure of Laccase From Cerrena Sp. RSD1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of Laccase From Cerrena Sp. RSD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu512

b:19.3
occ:1.00
O1 B:OXY513 1.9 45.5 1.0
NE2 B:HIS398 2.0 11.8 1.0
NE2 B:HIS448 2.1 14.0 1.0
NE2 B:HIS111 2.1 12.1 1.0
CE1 B:HIS398 2.8 11.3 1.0
O2 B:OXY513 2.9 61.9 1.0
CD2 B:HIS448 3.0 13.5 1.0
CE1 B:HIS111 3.0 12.0 1.0
CE1 B:HIS448 3.0 13.6 1.0
CD2 B:HIS111 3.1 11.7 1.0
CD2 B:HIS398 3.2 11.7 1.0
O B:HOH1026 3.6 19.1 1.0
CD2 B:HIS396 3.9 12.1 1.0
ND1 B:HIS398 4.0 11.8 1.0
ND1 B:HIS448 4.1 12.7 1.0
CG B:HIS448 4.1 12.7 1.0
ND1 B:HIS111 4.2 11.9 1.0
CG B:HIS398 4.2 11.5 1.0
CG B:HIS111 4.2 11.6 1.0
CU B:CU510 4.3 15.2 1.0
CD2 B:HIS64 4.4 11.8 1.0
CD2 B:PHE446 4.4 13.4 1.0
NE2 B:HIS396 4.5 12.0 1.0
NE2 B:HIS64 4.6 11.2 1.0
CB B:PHE446 4.7 12.7 1.0
CG B:PRO79 4.8 12.2 1.0
CE1 B:HIS109 4.8 11.0 1.0
NE2 B:HIS450 4.9 11.8 1.0
CU B:CU511 4.9 14.5 1.0

Reference:

M.H.Wu, C.C.Lee, A.S.Hsiao, S.M.Yu, A.H.J.Wang, T.D.Ho. Kinetic Analysis and Structural Studies of A High-Efficiency Laccase Fromcerrenasp. RSD1. Febs Open Bio V. 8 1230 2018.
ISSN: ESSN 2211-5463
PubMed: 30087829
DOI: 10.1002/2211-5463.12459
Page generated: Wed Jul 31 05:31:54 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy