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Zinc 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:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83F, PDB code: 1ibb:

Zinc binding site 1 out of 1 in 1ibb

Go back to Zinc Binding Sites List in 1ibb
Zinc 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 Zinc with other atoms in the Zn 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:Zn201

b:16.4
occ:1.00
OD1 A:ASP91 1.9 12.5 1.0
ND1 A:HIS70 2.1 16.3 1.0
ND1 A:HIS88 2.2 14.9 1.0
ND1 A:HIS79 2.2 10.1 1.0
CG A:ASP91 2.8 11.7 1.0
CE1 A:HIS70 3.0 16.5 1.0
OD2 A:ASP91 3.0 15.0 1.0
CG A:HIS88 3.1 11.8 1.0
CE1 A:HIS79 3.1 14.6 1.0
CG A:HIS70 3.1 17.1 1.0
CE1 A:HIS88 3.2 15.7 1.0
CG A:HIS79 3.3 16.0 1.0
CB A:HIS88 3.3 14.6 1.0
CB A:HIS70 3.5 14.8 1.0
CB A:HIS79 3.6 15.8 1.0
CA A:HIS79 3.8 17.8 1.0
NE2 A:HIS70 4.1 19.4 1.0
CB A:ASP91 4.1 11.1 1.0
CD2 A:HIS88 4.2 12.8 1.0
CD2 A:HIS70 4.2 16.5 1.0
NE2 A:HIS88 4.2 15.8 1.0
NE2 A:HIS79 4.3 14.4 1.0
CD2 A:HIS79 4.4 14.4 1.0
CA A:ASP91 4.6 9.6 1.0
CA A:HIS88 4.7 14.8 1.0
N A:GLY80 4.7 19.0 1.0
O A:LYS78 4.7 17.3 1.0
N A:ASP91 4.8 10.0 1.0
CD2 A:HIS45 4.8 14.0 1.0
C A:HIS79 4.8 18.8 1.0
N A:HIS79 4.9 16.5 1.0
N A:HIS88 4.9 11.7 1.0
CD2 A:LEU138 5.0 20.9 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 Dec 16 02:52:36 2020

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