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Copper in PDB 4n0m: Crystal Structure of Human C53A Dj-1 in Complex with Cu

Protein crystallography data

The structure of Crystal Structure of Human C53A Dj-1 in Complex with Cu, PDB code: 4n0m was solved by L.Cendron, S.Girotto, M.Bisaglia, I.Tessari, S.Mammi, G.Zanotti, L.Bubacco, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.58 / 1.95
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 75.140, 75.140, 75.271, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 17.5

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Human C53A Dj-1 in Complex with Cu (pdb code 4n0m). 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 Crystal Structure of Human C53A Dj-1 in Complex with Cu, PDB code: 4n0m:

Copper binding site 1 out of 1 in 4n0m

Go back to Copper Binding Sites List in 4n0m
Copper binding site 1 out of 1 in the Crystal Structure of Human C53A Dj-1 in Complex with Cu


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Human C53A Dj-1 in Complex with Cu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:21.2
occ:0.41
OE2 A:GLU18 2.0 21.6 1.0
SG A:CYS106 2.2 28.8 1.0
O A:HOH304 2.4 28.9 1.0
CD A:GLU18 2.9 23.9 1.0
CB A:CYS106 3.2 17.4 1.0
OE1 A:GLU18 3.2 16.6 1.0
CG A:GLU15 3.7 20.3 1.0
O A:HOH478 3.7 45.1 1.0
CD A:PRO158 3.8 13.8 1.0
N A:GLY75 3.9 14.5 1.0
CB A:GLU15 4.1 13.1 1.0
CG A:PRO158 4.2 14.9 1.0
O A:HOH452 4.2 42.4 1.0
CG A:GLU18 4.3 15.5 1.0
CA A:GLY75 4.5 15.8 1.0
CA A:CYS106 4.6 16.2 1.0
CA A:GLY157 4.6 11.7 1.0
N A:PRO158 4.6 12.9 1.0
C A:GLY74 4.7 14.7 1.0
O A:HOH477 4.7 33.7 1.0
CD2 A:HIS126 4.7 14.4 1.0
CD A:GLU15 4.8 18.0 1.0
CA A:GLY74 4.9 14.8 1.0
N A:ALA107 5.0 15.6 1.0

Reference:

S.Girotto, L.Cendron, M.Bisaglia, I.Tessari, S.Mammi, G.Zanotti, L.Bubacco. Dj-1 Is A Copper Chaperone Acting on SOD1 Activation. J.Biol.Chem. V. 289 10887 2014.
ISSN: ISSN 0021-9258
PubMed: 24567322
DOI: 10.1074/JBC.M113.535112
Page generated: Mon Jul 14 03:55:17 2025

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