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Copper in PDB 1adw: Pseudoazurin

Protein crystallography data

The structure of Pseudoazurin, PDB code: 1adw was solved by P.A.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 110.000, 58.400, 69.200, 90.00, 127.00, 90.00
R / Rfree (%) 18.9 / 23.9

Copper Binding Sites:

The binding sites of Copper atom in the Pseudoazurin (pdb code 1adw). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Pseudoazurin, PDB code: 1adw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1adw

Go back to Copper Binding Sites List in 1adw
Copper binding site 1 out of 2 in the Pseudoazurin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Pseudoazurin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu130

b:26.7
occ:1.00
ND1 A:HIS81 2.1 33.4 1.0
ND1 A:HIS40 2.1 9.6 1.0
SG A:CYS78 2.1 20.3 1.0
SD A:MET86 2.7 21.1 1.0
CE1 A:HIS81 3.0 29.3 1.0
CE1 A:HIS40 3.1 9.6 1.0
CB A:CYS78 3.1 18.5 1.0
CG A:HIS40 3.1 13.3 1.0
CG A:HIS81 3.2 27.8 1.0
CE A:MET86 3.5 20.9 1.0
CB A:HIS40 3.5 17.9 1.0
CB A:HIS81 3.6 18.5 1.0
CA A:HIS40 3.6 15.7 1.0
CG A:MET86 4.0 17.9 1.0
O A:SER39 4.0 14.8 1.0
NE2 A:HIS81 4.2 33.5 1.0
NE2 A:HIS40 4.3 10.3 1.0
CD2 A:HIS81 4.3 32.2 1.0
CD2 A:HIS40 4.3 9.5 1.0
N A:HIS40 4.4 21.0 1.0
CB A:MET86 4.5 15.8 1.0
CA A:CYS78 4.5 20.1 1.0
CG A:PRO80 4.5 20.9 1.0
N A:HIS81 4.5 25.0 1.0
C A:SER39 4.6 22.6 1.0
N A:ASN41 4.6 16.8 1.0
CA A:HIS81 4.7 17.5 1.0
C A:HIS40 4.7 18.6 1.0
O A:CYS78 4.9 22.4 1.0
C A:CYS78 4.9 21.9 1.0
OG A:SER39 5.0 37.6 1.0

Copper binding site 2 out of 2 in 1adw

Go back to Copper Binding Sites List in 1adw
Copper binding site 2 out of 2 in the Pseudoazurin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Pseudoazurin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu130

b:23.7
occ:1.00
ND1 B:HIS40 2.1 18.0 1.0
SG B:CYS78 2.1 19.9 1.0
ND1 B:HIS81 2.2 29.7 1.0
SD B:MET86 2.7 21.8 1.0
CE1 B:HIS81 3.0 28.6 1.0
CB B:CYS78 3.1 16.2 1.0
CE1 B:HIS40 3.1 17.6 1.0
CG B:HIS40 3.1 12.5 1.0
CG B:HIS81 3.2 26.9 1.0
CE B:MET86 3.4 13.2 1.0
CB B:HIS40 3.4 15.8 1.0
CB B:HIS81 3.6 21.4 1.0
CA B:HIS40 3.6 17.1 1.0
CG B:MET86 4.0 15.8 1.0
O B:SER39 4.1 28.5 1.0
NE2 B:HIS81 4.2 39.1 1.0
NE2 B:HIS40 4.3 20.2 1.0
CD2 B:HIS40 4.3 9.4 1.0
CD2 B:HIS81 4.3 31.2 1.0
N B:HIS40 4.4 26.3 1.0
CB B:MET86 4.5 15.3 1.0
CA B:CYS78 4.5 18.6 1.0
N B:HIS81 4.6 18.6 1.0
C B:SER39 4.6 24.0 1.0
CG B:PRO80 4.6 16.4 1.0
N B:ASN41 4.6 19.0 1.0
CA B:HIS81 4.7 18.7 1.0
C B:HIS40 4.7 17.8 1.0
O B:CYS78 4.9 21.1 1.0
C B:CYS78 4.9 19.1 1.0
OG B:SER39 5.0 23.2 1.0

Reference:

P.A.Williams, V.Fulop, Y.C.Leung, C.Chan, J.W.Moir, G.Howlett, S.J.Ferguson, S.E.Radford, J.Hajdu. Pseudospecific Docking Surfaces on Electron Transfer Proteins As Illustrated By Pseudoazurin, Cytochrome C550 and Cytochrome CD1 Nitrite Reductase. Nat.Struct.Biol. V. 2 975 1995.
ISSN: ISSN 1072-8368
PubMed: 7583671
DOI: 10.1038/NSB1195-975
Page generated: Wed Sep 2 21:32:38 2020
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