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Copper in PDB 3fpy: Azurin C112D/M121L

Protein crystallography data

The structure of Azurin C112D/M121L, PDB code: 3fpy 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) 24.22 / 2.10
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 48.620, 48.620, 276.311, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 23.6

Copper Binding Sites:

The binding sites of Copper atom in the Azurin C112D/M121L (pdb code 3fpy). 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/M121L, PDB code: 3fpy:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3fpy

Go back to Copper Binding Sites List in 3fpy
Copper binding site 1 out of 2 in the Azurin C112D/M121L


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Azurin C112D/M121L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu129

b:51.6
occ:1.00
N A:TRS131 1.9 26.7 1.0
N A:ALA1 2.4 23.7 1.0
O A:HOH267 2.7 31.0 1.0
C A:TRS131 2.8 28.8 1.0
O3 A:TRS131 3.0 30.6 1.0
O A:HOH217 3.0 37.0 1.0
C3 A:TRS131 3.0 28.9 1.0
C2 A:TRS131 3.4 27.2 1.0
O A:ALA1 3.5 30.8 1.0
CA A:ALA1 3.9 30.4 1.0
C1 A:TRS131 4.0 27.9 1.0
C A:ALA1 4.2 29.4 1.0
SG A:CYS3 4.3 28.0 1.0
O1 A:TRS131 4.4 29.6 1.0
OG A:SER25 4.4 28.1 1.0
O A:SER25 4.4 28.4 1.0
CB A:ALA1 4.7 27.7 1.0
O2 A:TRS131 4.7 27.1 1.0
O A:HOH236 4.8 27.7 1.0
C A:SER25 4.9 28.9 1.0

Copper binding site 2 out of 2 in 3fpy

Go back to Copper Binding Sites List in 3fpy
Copper binding site 2 out of 2 in the Azurin C112D/M121L


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Azurin C112D/M121L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu130

b:23.8
occ:1.00
OD2 A:ASP112 1.9 16.9 1.0
ND1 A:HIS46 1.9 17.0 1.0
ND1 A:HIS117 2.0 15.5 1.0
O A:GLY45 2.3 20.2 1.0
CE1 A:HIS46 2.8 19.2 1.0
CG A:ASP112 3.0 13.7 1.0
CE1 A:HIS117 3.0 18.0 1.0
CG A:HIS117 3.0 18.7 1.0
CG A:HIS46 3.1 16.9 1.0
C A:GLY45 3.3 19.8 1.0
CB A:HIS117 3.4 18.5 1.0
CA A:HIS46 3.4 18.0 1.0
OD1 A:ASP112 3.4 17.0 1.0
CB A:HIS46 3.6 16.4 1.0
N A:HIS46 3.7 18.4 1.0
CB A:PHE114 3.8 15.5 1.0
CD1 A:LEU121 3.8 19.0 1.0
NE2 A:HIS46 4.0 18.7 1.0
CD2 A:HIS46 4.1 15.7 1.0
NE2 A:HIS117 4.1 16.7 1.0
CD2 A:HIS117 4.2 16.4 1.0
CB A:ASP112 4.2 15.4 1.0
O A:MET44 4.4 21.2 1.0
CG A:PHE114 4.4 18.0 1.0
C A:MET44 4.5 21.1 1.0
CA A:GLY45 4.6 18.3 1.0
N A:GLY45 4.6 19.6 1.0
CD2 A:PHE114 4.7 20.1 1.0
CG A:LEU121 4.8 19.1 1.0
C A:HIS46 4.8 17.5 1.0
CA A:HIS117 4.8 19.7 1.0
CD2 A:LEU121 4.9 19.4 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: Sun Dec 13 11:09:38 2020

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