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Copper in PDB 2xjk: Monomeric Human Cu,Zn Superoxide Dismutase

Enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase

All present enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Monomeric Human Cu,Zn Superoxide Dismutase, PDB code: 2xjk was solved by K.Saraboji, L.Leinartaite, A.Nordlund, M.Oliveberg, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.160, 49.480, 80.440, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19.9

Other elements in 2xjk:

The structure of Monomeric Human Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Monomeric Human Cu,Zn Superoxide Dismutase (pdb code 2xjk). 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 Monomeric Human Cu,Zn Superoxide Dismutase, PDB code: 2xjk:

Copper binding site 1 out of 1 in 2xjk

Go back to Copper Binding Sites List in 2xjk
Copper binding site 1 out of 1 in the Monomeric Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Monomeric Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:32.0
occ:1.00
NE2 A:HIS48 2.1 17.4 1.0
NE2 A:HIS120 2.1 18.4 1.0
ND1 A:HIS46 2.1 20.2 1.0
O A:HOH2063 2.4 17.4 1.0
NE2 A:HIS63 2.8 17.1 1.0
CE1 A:HIS48 2.8 18.1 1.0
CE1 A:HIS120 3.0 18.5 1.0
CD2 A:HIS120 3.1 16.3 1.0
CE1 A:HIS46 3.1 20.0 1.0
CG A:HIS46 3.1 16.7 1.0
CD2 A:HIS48 3.2 18.0 1.0
CD2 A:HIS63 3.3 15.9 1.0
CB A:HIS46 3.4 14.9 1.0
CE1 A:HIS63 3.9 16.4 1.0
ND1 A:HIS48 4.0 18.8 1.0
ND1 A:HIS120 4.1 18.4 1.0
O A:HOH2147 4.1 33.4 1.0
CG A:HIS120 4.1 16.1 1.0
NE2 A:HIS46 4.2 20.6 1.0
CD2 A:HIS46 4.2 19.3 1.0
CG A:HIS48 4.2 14.8 1.0
O A:HOH2141 4.2 34.5 1.0
CG A:HIS63 4.5 13.9 1.0
CG1 A:VAL118 4.7 13.7 1.0
ND1 A:HIS63 4.7 14.6 1.0
CA A:HIS46 4.8 13.7 1.0
O A:THR137 4.9 16.6 1.0
CB A:VAL118 4.9 12.3 1.0

Reference:

L.Leinartaite, K.Saraboji, A.Nordlund, D.T.Logan, M.Oliveberg. Folding Catalysis By Transient Coordination of ZN2+ to the Cu Ligands of the Als-Associated Enzyme Cu/Zn Superoxide Dismutase 1. J.Am.Chem.Soc. V. 132 13495 2010.
ISSN: ISSN 0002-7863
PubMed: 20822138
DOI: 10.1021/JA1057136
Page generated: Wed Jul 31 00:10:17 2024

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