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Copper in PDB 1sxa: 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: 1sxa 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 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.890, 51.140, 148.150, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1sxa:

The structure of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

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 1sxa). 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: 1sxa:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1sxa

Go back to Copper Binding Sites List in 1sxa
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:21.4
occ:1.00
NE2 A:HIS118 2.2 11.9 1.0
ND1 A:HIS44 2.2 16.9 1.0
NE2 A:HIS46 2.2 9.8 1.0
NE2 A:HIS61 2.3 15.3 1.0
O A:HOH209 2.9 38.6 1.0
CE1 A:HIS118 3.0 13.7 1.0
CG A:HIS44 3.1 13.0 1.0
CE1 A:HIS46 3.1 7.6 1.0
CD2 A:HIS61 3.1 14.7 1.0
CD2 A:HIS118 3.1 14.1 1.0
O A:HOH268 3.2 52.3 1.0
CE1 A:HIS44 3.2 10.1 1.0
CB A:HIS44 3.2 8.5 1.0
CD2 A:HIS46 3.2 11.7 1.0
CE1 A:HIS61 3.3 11.6 1.0
ND1 A:HIS118 4.1 15.1 1.0
CG A:HIS118 4.2 12.8 1.0
ND1 A:HIS46 4.2 7.4 1.0
CD2 A:HIS44 4.2 10.8 1.0
CG A:HIS61 4.2 13.7 1.0
NE2 A:HIS44 4.3 12.6 1.0
ND1 A:HIS61 4.3 11.6 1.0
CG A:HIS46 4.3 7.4 1.0
CA A:HIS44 4.6 10.3 1.0
N A:HIS44 4.7 8.9 1.0
O A:HOH170 4.8 23.5 1.0
CB A:VAL116 4.8 11.0 1.0
CG1 A:VAL116 4.9 11.6 1.0
O A:HOH163 5.0 19.0 1.0
O A:HIS44 5.0 9.8 1.0

Copper binding site 2 out of 2 in 1sxa

Go back to Copper Binding Sites List in 1sxa
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:12.3
occ:1.00
NE2 B:HIS61 2.0 9.7 1.0
NE2 B:HIS118 2.1 5.7 1.0
ND1 B:HIS44 2.1 11.5 1.0
NE2 B:HIS46 2.3 8.7 1.0
O B:HOH164 2.5 14.6 1.0
CE1 B:HIS118 2.8 7.0 1.0
CE1 B:HIS61 2.9 9.7 1.0
CE1 B:HIS46 3.1 10.6 1.0
CG B:HIS44 3.1 9.6 1.0
CD2 B:HIS61 3.1 9.9 1.0
CE1 B:HIS44 3.1 10.5 1.0
CD2 B:HIS118 3.2 8.9 1.0
CD2 B:HIS46 3.3 6.1 1.0
CB B:HIS44 3.3 7.9 1.0
ND1 B:HIS118 4.0 6.4 1.0
ND1 B:HIS61 4.0 10.6 1.0
NE2 B:HIS44 4.2 10.3 1.0
CD2 B:HIS44 4.2 10.6 1.0
CG B:HIS61 4.2 7.5 1.0
CG B:HIS118 4.2 5.6 1.0
ND1 B:HIS46 4.2 9.7 1.0
CG B:HIS46 4.3 8.9 1.0
O B:HOH170 4.5 17.3 1.0
O B:HOH165 4.7 15.1 1.0
CA B:HIS44 4.7 5.2 1.0
N B:HIS44 4.9 8.7 1.0
CG1 B:VAL116 4.9 8.0 1.0
CB B:VAL116 5.0 5.8 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: Sun Dec 13 11:02:04 2020

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