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Copper in PDB 2c9u: 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase

Enzymatic activity of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase

All present enzymatic activity of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase, PDB code: 2c9u was solved by R.W.Strange, S.V.Antonyuk, M.A.Hough, P.A.Doucette, J.S.Valentine S, S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.19 / 1.24
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.638, 67.553, 52.320, 90.00, 106.48, 90.00
R / Rfree (%) 13.9 / 17.6

Copper Binding Sites:

The binding sites of Copper atom in the 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase (pdb code 2c9u). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase, PDB code: 2c9u:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2c9u

Go back to Copper Binding Sites List in 2c9u
Copper binding site 1 out of 2 in the 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1157

b:10.9
occ:0.45
ZN A:ZN1159 1.1 9.0 0.6
ND1 A:HIS46 1.8 11.7 1.0
NE2 A:HIS48 2.0 10.1 1.0
NE2 A:HIS120 2.2 10.5 1.0
CG A:HIS46 2.6 10.2 1.0
CB A:HIS46 2.8 11.8 1.0
CD2 A:HIS48 2.8 9.5 1.0
CE1 A:HIS46 3.0 12.9 1.0
CD2 A:HIS120 3.0 8.9 1.0
O1 A:SO41154 3.1 7.2 0.5
CE1 A:HIS48 3.2 11.2 1.0
CE1 A:HIS120 3.3 11.4 1.0
O A:HOH2193 3.4 27.8 0.6
CD2 A:HIS46 3.8 12.2 1.0
NE2 A:HIS63 3.9 14.2 1.0
O A:HOH2191 3.9 17.2 0.5
CB A:VAL118 4.0 7.8 1.0
NE2 A:HIS46 4.0 10.6 1.0
CA A:HIS46 4.0 7.6 1.0
CG A:HIS48 4.1 7.9 1.0
N A:HIS46 4.2 7.3 1.0
CD2 A:HIS63 4.2 13.8 1.0
ND1 A:HIS48 4.2 9.2 1.0
CG A:HIS120 4.2 9.0 1.0
CG1 A:VAL118 4.2 9.6 1.0
S A:SO41154 4.3 10.1 0.5
ND1 A:HIS120 4.4 10.3 1.0
O2 A:SO41154 4.4 9.9 0.5
O A:VAL118 4.5 8.8 1.0
O A:HIS46 4.5 7.5 1.0
C A:HIS46 4.5 6.5 1.0
CE1 A:HIS63 4.7 11.7 1.0
CG2 A:VAL118 4.7 8.4 1.0
C A:VAL118 4.9 7.5 1.0
C A:PHE45 5.0 6.8 1.0

Copper binding site 2 out of 2 in 2c9u

Go back to Copper Binding Sites List in 2c9u
Copper binding site 2 out of 2 in the 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu1156

b:9.5
occ:0.45
ZN F:ZN1155 0.8 11.5 0.6
ND1 F:HIS46 2.0 12.3 1.0
NE2 F:HIS120 2.0 10.1 1.0
NE2 F:HIS48 2.0 10.5 1.0
O1 F:SO41154 2.9 19.5 0.6
O F:HOH2190 2.9 11.6 0.5
CD2 F:HIS120 2.9 9.2 1.0
CG F:HIS46 2.9 11.0 1.0
CD2 F:HIS48 3.0 9.7 1.0
CE1 F:HIS46 3.0 12.6 1.0
CE1 F:HIS48 3.0 11.2 1.0
CE1 F:HIS120 3.1 10.9 1.0
CB F:HIS46 3.2 12.3 1.0
NE2 F:HIS63 3.6 13.9 1.0
O F:HOH2189 3.7 14.6 0.5
CD2 F:HIS63 3.8 14.1 1.0
CB F:VAL118 4.0 8.0 1.0
CG F:HIS120 4.1 9.4 1.0
CD2 F:HIS46 4.1 11.2 1.0
NE2 F:HIS46 4.1 11.5 1.0
ND1 F:HIS120 4.1 11.2 1.0
S F:SO41154 4.1 14.5 0.6
ND1 F:HIS48 4.1 9.8 1.0
CG F:HIS48 4.2 8.5 1.0
CG1 F:VAL118 4.2 10.4 1.0
O2 F:SO41154 4.2 16.5 0.6
CA F:HIS46 4.3 7.5 1.0
N F:HIS46 4.4 7.0 1.0
CE1 F:HIS63 4.5 10.4 1.0
O F:VAL118 4.6 8.4 1.0
CG2 F:VAL118 4.7 8.4 1.0
O F:HIS46 4.8 7.4 1.0
O4 F:SO41154 4.8 19.9 0.6
C F:HIS46 4.8 6.6 1.0
CG F:HIS63 4.9 10.7 1.0

Reference:

R.W.Strange, S.V.Antonyuk, M.A.Hough, P.A.Doucette, J.S.Valentine, S.S.Hasnain. Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and As-Isolated Wild-Type Enzymes. J.Mol.Biol. V. 356 1152 2006.
ISSN: ISSN 0022-2836
PubMed: 16406071
DOI: 10.1016/J.JMB.2005.11.081
Page generated: Thu Sep 3 16:32:30 2020
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