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Zinc in PDB 1ibh: X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I

Enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I

All present enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I:
1.15.1.1;

Protein crystallography data

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I, PDB code: 1ibh 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) 18.00 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 86.140, 86.140, 97.846, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 28.7

Other elements in 1ibh:

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I 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 M41I (pdb code 1ibh). 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 M41I, PDB code: 1ibh:

Zinc binding site 1 out of 1 in 1ibh

Go back to Zinc Binding Sites List in 1ibh
Zinc binding site 1 out of 1 in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I


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 M41I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:18.7
occ:1.00
OD1 A:ASP91 1.9 17.0 1.0
ND1 A:HIS79 2.2 14.2 1.0
ND1 A:HIS70 2.2 22.8 1.0
ND1 A:HIS88 2.3 18.5 1.0
CG A:ASP91 2.7 15.0 1.0
CE1 A:HIS79 2.9 10.6 1.0
OD2 A:ASP91 2.9 17.9 1.0
CE1 A:HIS70 3.2 24.5 1.0
CG A:HIS88 3.2 18.8 1.0
CG A:HIS70 3.2 25.1 1.0
CG A:HIS79 3.3 16.6 1.0
CE1 A:HIS88 3.3 21.8 1.0
CB A:HIS88 3.4 19.5 1.0
CB A:HIS70 3.5 21.9 1.0
CB A:HIS79 3.8 17.6 1.0
CA A:HIS79 3.9 20.0 1.0
CB A:ASP91 4.1 12.8 1.0
NE2 A:HIS79 4.1 13.7 1.0
NE2 A:HIS70 4.3 26.7 1.0
CD2 A:HIS79 4.3 14.2 1.0
CD2 A:HIS70 4.3 25.1 1.0
CD2 A:HIS88 4.4 20.8 1.0
NE2 A:HIS88 4.4 20.6 1.0
CA A:ASP91 4.6 13.3 1.0
O A:LYS78 4.6 23.7 1.0
N A:GLY80 4.7 17.1 1.0
CD2 A:HIS45 4.7 19.9 1.0
CA A:HIS88 4.8 21.5 1.0
N A:ASP91 4.8 16.0 1.0
C A:HIS79 4.8 19.7 1.0
N A:HIS79 4.9 22.3 1.0
CG A:HIS45 5.0 20.0 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 02:52:37 2020

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