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Copper in PDB 1ibd: X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A

Enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A

All present enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A:
1.15.1.1;

Protein crystallography data

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A, PDB code: 1ibd was solved by M.E.Stroppolo, A.Pesce, M.D'orazio, P.O'neill, D.Bordo, C.Rosano, M.Milani, A.Battistoni, M.Bolognesi, A.Desideri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 85.938, 85.938, 98.787, 90.00, 90.00, 120.00
R / Rfree (%) 21.4 / 26.9

Other elements in 1ibd:

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A (pdb code 1ibd). 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 X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A, PDB code: 1ibd:

Copper binding site 1 out of 1 in 1ibd

Go back to Copper Binding Sites List in 1ibd
Copper binding site 1 out of 1 in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant V29A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:18.0
occ:1.00
NE2 A:HIS125 2.1 15.6 1.0
ND1 A:HIS45 2.1 10.3 1.0
NE2 A:HIS47 2.3 17.6 1.0
CD2 A:HIS125 2.9 15.1 1.0
CE1 A:HIS45 3.0 9.7 1.0
CE1 A:HIS125 3.1 15.9 1.0
CG A:HIS45 3.1 12.4 1.0
NE2 A:HIS70 3.2 18.1 1.0
CD2 A:HIS47 3.3 13.5 1.0
CE1 A:HIS47 3.3 16.9 1.0
CB A:HIS45 3.4 9.1 1.0
CD2 A:HIS70 3.5 18.5 1.0
CB A:MET123 3.7 12.8 1.0
O A:HOH208 3.8 10.2 1.0
CG A:MET123 4.0 11.0 1.0
CG A:HIS125 4.1 12.0 1.0
ND1 A:HIS125 4.1 13.9 1.0
NE2 A:HIS45 4.2 9.9 1.0
CE1 A:HIS70 4.2 17.6 1.0
N A:HIS45 4.2 10.8 1.0
CD2 A:HIS45 4.2 12.2 1.0
CA A:HIS45 4.3 10.8 1.0
ND1 A:HIS47 4.4 17.3 1.0
CG A:HIS47 4.4 17.1 1.0
O A:HIS45 4.5 11.7 1.0
CG A:HIS70 4.6 17.8 1.0
C A:HIS45 4.6 11.8 1.0
O A:HOH227 4.6 17.4 1.0
O A:MET123 4.7 10.2 1.0
ND1 A:HIS70 4.9 17.6 1.0
CA A:MET123 4.9 13.4 1.0
C A:MET123 4.9 12.6 1.0

Reference:

M.E.Stroppolo, A.Pesce, M.D'orazio, P.O'neill, D.Bordo, C.Rosano, M.Milani, A.Battistoni, M.Bolognesi, A.Desideri. Single Mutations at the Subunit Interface Modulate Copper Reactivity in Photobacterium Leiognathi Cu,Zn Superoxide Dismutase. J.Mol.Biol. V. 308 555 2001.
ISSN: ISSN 0022-2836
PubMed: 11327787
DOI: 10.1006/JMBI.2001.4606
Page generated: Wed Oct 28 14:14:50 2020
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