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Copper in PDB 1bqk: Oxidized Pseudoazurin

Protein crystallography data

The structure of Oxidized Pseudoazurin, PDB code: 1bqk was solved by T.Inoue, N.Nishio, S.Hamanaka, T.Shimomura, S.Harada, S.Suzuki, T.Kohzuma, S.Shidara, H.Iwasaki, Y.Kai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.731, 61.544, 30.083, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 19

Copper Binding Sites:

The binding sites of Copper atom in the Oxidized Pseudoazurin (pdb code 1bqk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Oxidized Pseudoazurin, PDB code: 1bqk:

Copper binding site 1 out of 1 in 1bqk

Go back to Copper Binding Sites List in 1bqk
Copper binding site 1 out of 1 in the Oxidized Pseudoazurin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Oxidized Pseudoazurin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu125

b:5.4
occ:1.00
ND1 A:HIS81 1.9 2.4 1.0
ND1 A:HIS40 2.0 3.6 1.0
SG A:CYS78 2.1 4.4 1.0
SD A:MET86 2.7 4.7 1.0
CE1 A:HIS81 2.9 5.0 1.0
CE1 A:HIS40 2.9 5.7 1.0
CG A:HIS40 3.0 3.0 1.0
CG A:HIS81 3.0 4.1 1.0
CB A:CYS78 3.2 2.5 1.0
CB A:HIS81 3.4 4.0 1.0
CB A:HIS40 3.4 4.2 1.0
CE A:MET86 3.5 7.8 1.0
CA A:HIS40 3.7 3.7 1.0
O A:GLY39 3.9 6.8 1.0
NE2 A:HIS81 4.0 6.7 1.0
NE2 A:HIS40 4.1 4.9 1.0
CD2 A:HIS40 4.1 4.2 1.0
CG A:MET86 4.1 3.9 1.0
CD2 A:HIS81 4.1 5.5 1.0
CG A:PRO80 4.4 5.4 1.0
N A:HIS81 4.5 2.8 1.0
N A:HIS40 4.5 3.9 1.0
CA A:CYS78 4.6 3.6 1.0
CB A:MET86 4.6 3.1 1.0
C A:GLY39 4.6 4.0 1.0
CA A:HIS81 4.6 3.1 1.0
N A:ASN41 4.7 4.5 1.0
C A:HIS40 4.7 3.1 1.0
C A:CYS78 5.0 3.9 1.0
SD A:MET16 5.0 8.0 1.0

Reference:

T.Inoue, N.Nishio, S.Suzuki, K.Kataoka, T.Kohzuma, Y.Kai. Crystal Structure Determinations of Oxidized and Reduced Pseudoazurins From Achromobacter Cycloclastes. Concerted Movement of Copper Site in Redox Forms with the Rearrangement of Hydrogen Bond at A Remote Histidine. J.Biol.Chem. V. 274 17845 1999.
ISSN: ISSN 0021-9258
PubMed: 10364229
DOI: 10.1074/JBC.274.25.17845
Page generated: Wed Oct 28 14:13:57 2020
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