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Copper in PDB 2rac: Amicyanin Reduced, pH 7.7, 1.3 Angstroms

Protein crystallography data

The structure of Amicyanin Reduced, pH 7.7, 1.3 Angstroms, PDB code: 2rac was solved by L.M.Cunane, Z.-W.Chen, R.C.E.Durley, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 28.750, 56.200, 27.420, 90.00, 96.12, 90.00
R / Rfree (%) 18.2 / 21

Copper Binding Sites:

The binding sites of Copper atom in the Amicyanin Reduced, pH 7.7, 1.3 Angstroms (pdb code 2rac). 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 Amicyanin Reduced, pH 7.7, 1.3 Angstroms, PDB code: 2rac:

Copper binding site 1 out of 1 in 2rac

Go back to Copper Binding Sites List in 2rac
Copper binding site 1 out of 1 in the Amicyanin Reduced, pH 7.7, 1.3 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Amicyanin Reduced, pH 7.7, 1.3 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu107

b:19.5
occ:1.00
ND1 A:HIS53 1.9 9.7 1.0
SG A:CYS92 2.1 10.5 1.0
CE1 A:HIS53 2.9 10.1 1.0
CG A:HIS53 2.9 10.8 1.0
SD A:MET98 2.9 10.6 1.0
CB A:CYS92 3.1 7.9 1.0
CB A:HIS53 3.2 9.2 1.0
CD2 A:HIS95 3.4 18.8 1.0
CA A:HIS53 3.5 9.4 1.0
CE A:MET98 3.7 10.3 1.0
CB A:HIS95 4.0 13.2 1.0
NE2 A:HIS53 4.0 11.7 1.0
CG A:HIS95 4.0 15.9 1.0
CD2 A:HIS53 4.0 11.2 1.0
O A:PRO52 4.1 13.1 1.0
N A:ASN54 4.3 8.0 1.0
CG A:MET98 4.4 9.9 1.0
CA A:CYS92 4.5 8.4 1.0
C A:HIS53 4.5 9.4 1.0
CG A:PRO94 4.6 12.2 1.0
N A:HIS53 4.6 10.7 1.0
NE2 A:HIS95 4.6 19.0 1.0
C A:PRO52 4.7 13.1 1.0
CB A:MET98 4.8 9.5 1.0
N A:HIS95 4.9 10.2 1.0
O A:ASN54 4.9 8.9 1.0
O A:HIS95 4.9 10.6 1.0
CA A:HIS95 5.0 11.2 1.0

Reference:

Z.Zhu, L.M.Cunane, Z.Chen, R.C.Durley, F.S.Mathews, V.L.Davidson. Molecular Basis For Interprotein Complex-Dependent Effects on the Redox Properties of Amicyanin. Biochemistry V. 37 17128 1998.
ISSN: ISSN 0006-2960
PubMed: 9860825
DOI: 10.1021/BI9817919
Page generated: Thu Sep 3 16:50:16 2020
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