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Copper in PDB 3l45: A Joint Neutron and X-Ray Structure of Oxidized Amicyanin

Protein crystallography data

The structure of A Joint Neutron and X-Ray Structure of Oxidized Amicyanin, PDB code: 3l45 was solved by N.Sukumar, F.S.Mathews, P.Langan, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 27.540, 56.580, 28.860, 90.00, 96.21, 90.00
R / Rfree (%) 19.8 / 21.5

Copper Binding Sites:

The binding sites of Copper atom in the A Joint Neutron and X-Ray Structure of Oxidized Amicyanin (pdb code 3l45). 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 A Joint Neutron and X-Ray Structure of Oxidized Amicyanin, PDB code: 3l45:

Copper binding site 1 out of 1 in 3l45

Go back to Copper Binding Sites List in 3l45
Copper binding site 1 out of 1 in the A Joint Neutron and X-Ray Structure of Oxidized Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of A Joint Neutron and X-Ray Structure of Oxidized Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu107

b:23.0
occ:1.00
ND1 A:HIS53 2.0 16.2 1.0
SG A:CYS92 2.1 16.6 1.0
ND1 A:HIS95 2.4 23.9 1.0
HG A:CYS92 2.8 14.7 0.3
DG A:CYS92 2.8 14.7 0.7
HB2 A:HIS95 2.8 18.4 1.0
SD A:MET98 2.8 19.3 1.0
HB3 A:HIS53 2.9 16.5 1.0
CE1 A:HIS53 3.0 18.6 1.0
HA A:HIS53 3.0 14.7 1.0
CG A:HIS53 3.0 18.0 1.0
CB A:CYS92 3.1 14.5 1.0
HB2 A:CYS92 3.2 14.2 1.0
HE1 A:HIS53 3.2 17.2 1.0
CE1 A:HIS95 3.3 23.6 1.0
HB3 A:CYS92 3.3 14.8 1.0
CB A:HIS53 3.3 15.6 1.0
HE1 A:HIS95 3.4 24.0 1.0
CG A:HIS95 3.4 19.4 1.0
HE1 A:MET98 3.4 18.8 1.0
HG2 A:PRO94 3.5 17.5 1.0
CE A:MET98 3.6 20.4 1.0
CB A:HIS95 3.6 17.4 1.0
CA A:HIS53 3.7 17.2 1.0
H A:ASN54 3.7 13.3 1.0
HE2 A:MET98 3.9 19.4 1.0
NE2 A:HIS53 4.1 19.1 1.0
O A:PRO52 4.1 21.2 1.0
H A:HIS95 4.1 17.7 0.8
D A:HIS95 4.1 17.7 0.2
CD2 A:HIS53 4.2 19.3 1.0
HE2 A:MET28 4.2 27.5 1.0
HB2 A:MET98 4.2 16.6 1.0
HB3 A:HIS95 4.3 16.3 1.0
CG A:MET98 4.4 17.3 1.0
HB2 A:HIS53 4.4 16.2 1.0
NE2 A:HIS95 4.4 21.2 1.0
HD2 A:PRO94 4.5 16.3 1.0
CD2 A:HIS95 4.5 21.6 1.0
HG3 A:MET98 4.5 16.7 1.0
N A:ASN54 4.5 14.6 1.0
CA A:CYS92 4.5 14.0 1.0
CG A:PRO94 4.5 17.0 1.0
N A:HIS95 4.6 17.3 1.0
HE3 A:MET98 4.6 19.2 1.0
C A:HIS53 4.7 16.1 1.0
N A:HIS53 4.7 17.8 1.0
CA A:HIS95 4.7 17.9 1.0
CB A:MET98 4.8 15.8 1.0
C A:PRO52 4.8 19.4 1.0
O A:HIS95 4.8 18.3 1.0
HG3 A:MET51 4.9 31.4 1.0
HA A:CYS92 4.9 11.2 1.0
HG3 A:PRO94 4.9 17.1 1.0
HE1 A:MET71 4.9 24.8 1.0
HG23 A:ILE25 4.9 19.4 1.0
DE2 A:HIS53 5.0 17.3 1.0
HE2 A:HIS53 5.0 17.3 0.0

Reference:

N.Sukumar, F.S.Mathews, P.Langan, V.L.Davidson. A Joint X-Ray and Neutron Study on Amicyanin Reveals the Role of Protein Dynamics in Electron Transfer. Proc.Natl.Acad.Sci.Usa V. 107 6817 2010.
ISSN: ISSN 0027-8424
PubMed: 20351252
DOI: 10.1073/PNAS.0912672107
Page generated: Wed Oct 28 14:24:30 2020
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