Atomistry » Copper » PDB 2aps-2cg1 » 2c9u
Atomistry »
  Copper »
    PDB 2aps-2cg1 »
      2c9u »

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

Other elements in 2c9u:

The structure of 1.24 Angstroms Resolution Structure of As-Isolated Cu-Zn Human Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

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: Tue Jul 30 23:17:56 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy