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Copper in PDB 1ibb: X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F

Enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F

All present enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F:
1.15.1.1;

Protein crystallography data

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F, PDB code: 1ibb 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 / 2.10
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 87.120, 87.120, 98.392, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 21

Other elements in 1ibb:

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F 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 W83F (pdb code 1ibb). 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 W83F, PDB code: 1ibb:

Copper binding site 1 out of 1 in 1ibb

Go back to Copper Binding Sites List in 1ibb
Copper binding site 1 out of 1 in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F


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 W83F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:27.1
occ:1.00
ND1 A:HIS45 2.1 14.4 1.0
NE2 A:HIS125 2.1 16.7 1.0
NE2 A:HIS47 2.2 11.1 1.0
NE2 A:HIS70 2.7 19.4 1.0
CE1 A:HIS45 3.0 14.8 1.0
CD2 A:HIS125 3.1 16.4 1.0
CE1 A:HIS125 3.1 19.6 1.0
CG A:HIS45 3.1 11.4 1.0
CD2 A:HIS47 3.1 12.9 1.0
CD2 A:HIS70 3.2 16.5 1.0
CE1 A:HIS47 3.2 15.3 1.0
CB A:HIS45 3.5 10.8 1.0
O A:HOH209 3.6 31.1 1.0
CE1 A:HIS70 3.8 16.5 1.0
CB A:MET123 4.0 16.1 1.0
NE2 A:HIS45 4.1 15.1 1.0
ND1 A:HIS125 4.2 19.9 1.0
CD2 A:HIS45 4.2 14.0 1.0
CG A:HIS125 4.2 16.7 1.0
O A:HOH223 4.2 38.5 1.0
CG A:MET123 4.3 15.7 1.0
CG A:HIS47 4.3 14.6 1.0
ND1 A:HIS47 4.3 14.9 1.0
CG A:HIS70 4.4 17.1 1.0
CA A:HIS45 4.4 10.6 1.0
N A:HIS45 4.5 12.3 1.0
ND1 A:HIS70 4.7 16.3 1.0
O A:HIS45 4.7 11.2 1.0
C A:HIS45 4.8 9.5 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: Sun Dec 13 10:59:21 2020

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