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Copper in PDB 3fq1: Azurin C112D/M121I

Protein crystallography data

The structure of Azurin C112D/M121I, PDB code: 3fq1 was solved by K.M.Lancaster, H.B.Gray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.99 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 48.500, 54.800, 95.780, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 25.6

Copper Binding Sites:

The binding sites of Copper atom in the Azurin C112D/M121I (pdb code 3fq1). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Azurin C112D/M121I, PDB code: 3fq1:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3fq1

Go back to Copper Binding Sites List in 3fq1
Copper binding site 1 out of 2 in the Azurin C112D/M121I


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Azurin C112D/M121I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu129

b:30.3
occ:0.75
N A:ALA1 2.0 24.0 1.0
N A:TRS131 2.1 21.6 1.0
O A:ALA1 2.1 22.3 1.0
O3 A:TRS131 2.4 20.4 1.0
O A:HOH153 2.4 19.1 1.0
C A:ALA1 2.9 23.1 1.0
CA A:ALA1 2.9 23.6 1.0
C A:TRS131 3.0 21.2 1.0
C3 A:TRS131 3.1 19.1 1.0
CB A:ALA1 3.6 23.8 1.0
C1 A:TRS131 3.7 22.1 1.0
N A:GLU2 4.2 21.7 1.0
OG A:SER25 4.3 24.2 1.0
C2 A:TRS131 4.3 21.7 1.0
O1 A:TRS131 4.4 24.8 1.0
SG A:CYS3 4.4 21.4 1.0
O A:HOH185 4.5 28.6 1.0
CA A:GLU2 4.9 25.0 1.0

Copper binding site 2 out of 2 in 3fq1

Go back to Copper Binding Sites List in 3fq1
Copper binding site 2 out of 2 in the Azurin C112D/M121I


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Azurin C112D/M121I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu130

b:29.6
occ:1.00
ND1 A:HIS46 2.0 20.4 1.0
OD2 A:ASP112 2.1 27.7 1.0
ND1 A:HIS117 2.1 24.2 1.0
O A:GLY45 2.5 19.6 1.0
CG A:ASP112 2.8 24.1 1.0
CE1 A:HIS46 3.0 19.5 1.0
CE1 A:HIS117 3.0 25.7 1.0
CG A:HIS46 3.0 19.6 1.0
OD1 A:ASP112 3.1 23.5 1.0
CG A:HIS117 3.1 26.9 1.0
CA A:HIS46 3.2 20.5 1.0
CB A:HIS46 3.4 20.8 1.0
C A:GLY45 3.5 21.4 1.0
CB A:HIS117 3.5 23.4 1.0
CD1 A:ILE121 3.7 25.7 1.0
N A:HIS46 3.7 20.4 1.0
CB A:PHE114 4.0 21.3 1.0
CB A:ASP112 4.0 20.0 1.0
NE2 A:HIS46 4.1 24.8 1.0
CD2 A:HIS46 4.1 19.1 1.0
NE2 A:HIS117 4.2 24.5 1.0
CD2 A:HIS117 4.2 24.2 1.0
C A:HIS46 4.5 20.6 1.0
CG A:PHE114 4.7 25.2 1.0
N A:ASN47 4.7 20.0 1.0
CA A:GLY45 4.8 22.4 1.0
CE1 A:PHE15 4.9 28.3 1.0
N A:GLY45 4.9 22.6 1.0
CD2 A:PHE114 5.0 26.2 1.0

Reference:

K.M.Lancaster, S.Debeer George, K.Yokoyama, J.H.Richards, H.B.Gray. Type Zero Copper Proteins. Nat Chem V. 1 711 2009.
ISSN: ISSN 1755-4349
PubMed: 20305734
DOI: 10.1038/NCHEM.412
Page generated: Wed Oct 28 14:23:51 2020
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