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Copper in PDB 1bzo: Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography.

Enzymatic activity of Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography.

All present enzymatic activity of Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography.:
1.15.1.1;

Protein crystallography data

The structure of Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography., PDB code: 1bzo was solved by D.Bordo, D.Matak, K.Djinovic-Carugo, C.Rosano, A.Pesce, M.Bolognesi, M.E.Stroppolo, M.Falconi, A.Battistoni, A.Desideri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.70 / 2.10
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 86.890, 86.890, 99.010, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 26

Copper Binding Sites:

The binding sites of Copper atom in the Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography. (pdb code 1bzo). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography., PDB code: 1bzo:

Copper binding site 1 out of 1 in 1bzo

Go back to Copper Binding Sites List in 1bzo
Copper binding site 1 out of 1 in the Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Three-Dimensional Structure of Prokaryotic Cu,Zn Superoxide Dismutase From P.Leiognathi, Solved By X-Ray Crystallography. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu152

b:28.4
occ:1.00
 NE2 A:HIS46 2.0 20.2 1.0
ND1 A:HIS44 2.1 16.5 1.0
NE2 A:HIS118 2.2 15.6 1.0
CD2 A:HIS46 3.0 17.1 1.0
CE1 A:HIS46 3.1 19.7 1.0
CG A:HIS44 3.1 12.9 1.0
CD2 A:HIS118 3.1 13.7 1.0
CE1 A:HIS44 3.1 12.8 1.0
NE2 A:HIS61 3.2 27.0 1.0
CE1 A:HIS118 3.2 15.9 1.0
CB A:HIS44 3.4 6.0 1.0
O A:HOH533 3.5 23.2 1.0
CD2 A:HIS61 3.5 24.5 1.0
CB A:MET116 3.8 15.2 1.0
CG A:MET116 4.1 14.6 1.0
CG A:HIS46 4.1 16.9 1.0
CE1 A:HIS61 4.2 24.0 1.0
ND1 A:HIS46 4.2 21.9 1.0
CG A:HIS118 4.3 15.1 1.0
CD2 A:HIS44 4.3 19.3 1.0
NE2 A:HIS44 4.3 15.8 1.0
ND1 A:HIS118 4.3 17.9 1.0
N A:HIS44 4.4 21.1 1.0
CA A:HIS44 4.4 11.1 1.0
O A:HOH526 4.4 19.3 1.0
CG A:HIS61 4.6 24.6 1.0
O A:HIS44 4.7 20.8 1.0
C A:HIS44 4.8 16.3 1.0
O A:MET116 4.8 15.7 1.0
ND1 A:HIS61 5.0 25.4 1.0

Reference:

D.Bordo, D.Matak, K.Djinovic-Carugo, C.Rosano, A.Pesce, M.Bolognesi, M.E.Stroppolo, M.Falconi, A.Battistoni, A.Desideri. Evolutionary Constraints For Dimer Formation in Prokaryotic Cu,Zn Superoxide Dismutase. J.Mol.Biol. V. 285 283 1999.
ISSN: ISSN 0022-2836
PubMed: 9878406
DOI: 10.1006/JMBI.1998.2267
Page generated: Wed Sep 2 21:38:41 2020
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