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Zinc 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:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Monomeric Human Cu,Zn Superoxide Dismutase (pdb code 2xjk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Monomeric Human Cu,Zn Superoxide Dismutase, PDB code: 2xjk:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2xjk

Go back to Zinc Binding Sites List in 2xjk
Zinc binding site 1 out of 4 in the Monomeric Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Monomeric Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:13.2
occ:1.00
ND1 A:HIS63 2.0 14.6 1.0
OD1 A:ASP83 2.0 12.8 1.0
ND1 A:HIS80 2.0 12.3 1.0
ND1 A:HIS71 2.0 13.1 1.0
CG A:ASP83 2.8 13.5 1.0
CE1 A:HIS71 2.9 12.9 1.0
OD2 A:ASP83 2.9 13.9 1.0
CE1 A:HIS80 2.9 12.4 1.0
CE1 A:HIS63 2.9 16.4 1.0
CG A:HIS63 3.1 13.9 1.0
CG A:HIS80 3.1 11.4 1.0
CG A:HIS71 3.2 13.4 1.0
CB A:HIS63 3.5 14.2 1.0
CB A:HIS80 3.5 12.3 1.0
CB A:HIS71 3.6 13.3 1.0
O A:LYS136 3.9 16.5 1.0
CA A:HIS71 4.0 13.9 1.0
NE2 A:HIS80 4.0 14.1 1.0
NE2 A:HIS63 4.1 17.1 1.0
NE2 A:HIS71 4.1 14.4 1.0
CD2 A:HIS80 4.1 11.9 1.0
CD2 A:HIS63 4.1 15.9 1.0
CB A:ASP83 4.2 13.6 1.0
CD2 A:HIS71 4.2 13.4 1.0
CA A:ASP83 4.7 13.9 1.0
N A:HIS80 4.7 13.8 1.0
N A:GLY72 4.7 15.2 1.0
CA A:HIS80 4.7 13.2 1.0
C A:LYS136 4.9 16.3 1.0
N A:ASP83 4.9 13.9 1.0
C A:HIS71 4.9 14.9 1.0
N A:HIS71 5.0 14.8 1.0
CA A:HIS63 5.0 14.7 1.0

Zinc binding site 2 out of 4 in 2xjk

Go back to Zinc Binding Sites List in 2xjk
Zinc binding site 2 out of 4 in the Monomeric Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Monomeric Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn156

b:15.0
occ:1.00
OE2 A:GLU51 2.0 14.9 1.0
O A:HOH2153 2.0 16.6 1.0
CD A:GLU51 3.0 14.4 1.0
CG A:GLU51 3.5 16.1 1.0
OD1 A:ASP52 3.9 20.8 1.0
OE1 A:GLU51 4.1 16.2 1.0
O A:HOH2121 4.5 36.5 1.0
CG A:ASP52 4.8 21.1 1.0
OD2 A:ASP52 4.8 19.4 1.0
CB A:GLU51 4.9 15.7 1.0

Zinc binding site 3 out of 4 in 2xjk

Go back to Zinc Binding Sites List in 2xjk
Zinc binding site 3 out of 4 in the Monomeric Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Monomeric Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn157

b:21.3
occ:1.00
OE2 A:GLU50 1.9 18.7 1.0
OD2 A:ASP52 1.9 19.4 1.0
CD A:GLU50 2.8 19.4 1.0
OE1 A:GLU50 2.9 22.9 1.0
CG A:ASP52 2.9 21.1 1.0
CB A:ASP52 3.3 21.2 1.0
OD1 A:ASP52 4.1 20.8 1.0
N A:ASP52 4.1 18.9 1.0
CG A:GLU50 4.2 17.9 1.0
CA A:ASP52 4.3 21.4 1.0
O A:HOH2054 4.4 55.3 1.0
O A:HOH2153 4.5 16.6 1.0
OG A:SER59 4.6 54.3 0.5
N A:GLU51 4.7 15.0 1.0
CA A:GLU50 5.0 15.0 1.0

Zinc binding site 4 out of 4 in 2xjk

Go back to Zinc Binding Sites List in 2xjk
Zinc binding site 4 out of 4 in the Monomeric Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Monomeric Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn158

b:41.1
occ:0.40
NE2 A:HIS110 1.9 28.0 1.0
CE1 A:HIS110 2.8 29.4 1.0
CD2 A:HIS110 2.9 26.4 1.0
O A:HOH2118 3.7 55.4 1.0
ND1 A:HIS110 3.9 28.8 1.0
CG A:HIS110 4.0 24.0 1.0
O A:PRO66 4.8 22.6 1.0
O A:HOH2122 4.9 35.2 1.0
CB A:PRO66 4.9 19.6 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 Dec 16 03:59:58 2020

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