Zinc in PDB 1ib5: X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y

All present enzymatic activity of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y:
1.15.1.1;

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y, PDB code: 1ib5 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)	20.00 / 2.45
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	87.336, 87.336, 98.223, 90.00, 90.00, 120.00
R / Rfree (%)	21.6 / 26.5

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y also contains other interesting chemical elements:

Copper

(Cu)

1 atom

The binding sites of Zinc atom in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y (pdb code 1ib5). 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 W83Y, PDB code: 1ib5:

Zinc binding site 1 out of 1 in the X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant W83Y


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 W83Y within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:21.6 occ:1.00 OD1 A:ASP91 1.9 19.6 1.0 ND1 A:HIS70 2.1 19.4 1.0 ND1 A:HIS79 2.2 14.5 1.0 ND1 A:HIS88 2.2 18.8 1.0 CG A:ASP91 2.9 19.1 1.0 CE1 A:HIS70 3.0 21.0 1.0 CG A:HIS88 3.1 18.9 1.0 CE1 A:HIS79 3.1 15.6 1.0 CG A:HIS70 3.1 20.1 1.0 OD2 A:ASP91 3.2 22.1 1.0 CG A:HIS79 3.3 15.5 1.0 CE1 A:HIS88 3.3 17.2 1.0 CB A:HIS88 3.3 21.2 1.0 CB A:HIS70 3.5 19.7 1.0 CB A:HIS79 3.6 17.5 1.0 CA A:HIS79 3.8 19.5 1.0 NE2 A:HIS70 4.1 20.2 1.0 CD2 A:HIS70 4.2 19.2 1.0 CB A:ASP91 4.2 20.4 1.0 NE2 A:HIS79 4.3 16.3 1.0 CD2 A:HIS88 4.3 16.9 1.0 NE2 A:HIS88 4.3 18.8 1.0 CD2 A:HIS79 4.4 15.4 1.0 CD2 A:LEU138 4.6 23.4 1.0 CA A:ASP91 4.6 19.9 1.0 O A:LYS78 4.6 25.3 1.0 N A:GLY80 4.6 18.4 1.0 CA A:HIS88 4.7 22.7 1.0 C A:HIS79 4.8 18.5 1.0 N A:HIS79 4.8 21.9 1.0 N A:ASP91 4.8 21.7 1.0

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