Atomistry » Copper » PDB 1oe2-1rjp » 1sxb
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1sxb »

Copper in PDB 1sxb: Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution

Enzymatic activity of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution

All present enzymatic activity of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution, PDB code: 1sxb was solved by W.R.Rypniewski, S.Mangani, B.Bruni, P.Orioli, M.Casati, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.710, 50.980, 147.820, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution (pdb code 1sxb). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution, PDB code: 1sxb:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1sxb

Go back to Copper Binding Sites List in 1sxb
Copper binding site 1 out of 2 in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution


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 Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu152

b:21.9
occ:1.00
ND1 A:HIS44 2.1 11.3 1.0
NE2 A:HIS118 2.2 11.0 1.0
NE2 A:HIS46 2.2 9.6 1.0
NE2 A:HIS61 2.4 18.9 1.0
CE1 A:HIS46 3.0 6.0 1.0
CG A:HIS44 3.0 10.5 1.0
O A:HOH258 3.0 47.7 1.0
CE1 A:HIS118 3.1 6.9 1.0
CE1 A:HIS44 3.1 8.2 1.0
CD2 A:HIS118 3.1 10.7 1.0
CD2 A:HIS61 3.2 13.5 1.0
CD2 A:HIS46 3.3 6.9 1.0
CB A:HIS44 3.3 4.1 1.0
CE1 A:HIS61 3.4 9.8 1.0
O A:HOH195 3.4 32.7 1.0
CD2 A:HIS44 4.1 6.4 1.0
ND1 A:HIS118 4.2 11.7 1.0
NE2 A:HIS44 4.2 11.0 1.0
ND1 A:HIS46 4.2 8.3 1.0
CG A:HIS118 4.2 11.7 1.0
CG A:HIS61 4.3 11.1 1.0
CG A:HIS46 4.3 5.5 1.0
ND1 A:HIS61 4.4 11.1 1.0
CA A:HIS44 4.6 8.8 1.0
N A:HIS44 4.6 6.8 1.0
CG1 A:VAL116 4.7 8.9 1.0
CB A:VAL116 4.7 8.8 1.0
O A:HOH180 4.8 26.8 1.0
O A:HIS44 5.0 8.1 1.0

Copper binding site 2 out of 2 in 1sxb

Go back to Copper Binding Sites List in 1sxb
Copper binding site 2 out of 2 in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:14.3
occ:1.00
NE2 B:HIS61 2.1 12.1 1.0
ND1 B:HIS44 2.1 13.8 1.0
NE2 B:HIS118 2.1 8.5 1.0
NE2 B:HIS46 2.2 8.2 1.0
O B:HOH172 2.6 16.9 1.0
CE1 B:HIS118 2.9 4.8 1.0
CE1 B:HIS46 3.0 8.2 1.0
CE1 B:HIS44 3.0 12.8 1.0
CG B:HIS44 3.0 11.0 1.0
CD2 B:HIS61 3.1 13.2 1.0
CE1 B:HIS61 3.1 11.3 1.0
CD2 B:HIS118 3.2 12.2 1.0
CD2 B:HIS46 3.3 8.3 1.0
CB B:HIS44 3.3 7.0 1.0
ND1 B:HIS118 4.0 8.4 1.0
NE2 B:HIS44 4.1 10.4 1.0
ND1 B:HIS46 4.1 10.6 1.0
CD2 B:HIS44 4.1 9.5 1.0
ND1 B:HIS61 4.1 11.5 1.0
CG B:HIS61 4.2 11.9 1.0
CG B:HIS118 4.2 6.5 1.0
CG B:HIS46 4.3 10.7 1.0
O B:HOH169 4.4 16.1 1.0
CA B:HIS44 4.7 6.2 1.0
O B:HOH166 4.7 14.2 1.0
N B:HIS44 4.9 6.7 1.0
CG1 B:VAL116 4.9 7.6 1.0
CB B:VAL116 5.0 7.5 1.0

Reference:

W.R.Rypniewski, S.Mangani, B.Bruni, P.L.Orioli, M.Casati, K.S.Wilson. Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 A Resolution. J.Mol.Biol. V. 251 282 1995.
ISSN: ISSN 0022-2836
PubMed: 7643403
DOI: 10.1006/JMBI.1995.0434
Page generated: Thu Sep 3 16:19:51 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy