Copper in PDB 1ibh: 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;

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

The structure of X-Ray 3D Structure of P.Leiognathi Cu,Zn Sod Mutant M41I also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Copper 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 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 M41I, PDB code: 1ibh:

Copper 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 Copper with other atoms in the Cu 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:Cu202 b:31.0 occ:1.00 ND1 A:HIS45 2.2 21.2 1.0 NE2 A:HIS47 2.2 26.7 1.0 NE2 A:HIS125 2.2 33.2 1.0 NE2 A:HIS70 2.6 26.7 1.0 CD2 A:HIS125 3.0 33.2 1.0 CG A:HIS45 3.1 20.0 1.0 CD2 A:HIS70 3.1 25.1 1.0 CE1 A:HIS47 3.2 25.6 1.0 CD2 A:HIS47 3.2 22.9 1.0 CE1 A:HIS45 3.2 18.6 1.0 CE1 A:HIS125 3.3 34.0 1.0 CB A:HIS45 3.4 16.2 1.0 O A:HOH211 3.4 22.1 1.0 CE1 A:HIS70 3.6 24.5 1.0 CB A:MET123 4.0 18.9 1.0 CG A:MET123 4.2 21.4 1.0 CG A:HIS125 4.2 31.3 1.0 CG A:HIS70 4.2 25.1 1.0 CD2 A:HIS45 4.3 19.9 1.0 O A:HOH224 4.3 26.8 1.0 NE2 A:HIS45 4.3 21.4 1.0 ND1 A:HIS47 4.3 24.7 1.0 CA A:HIS45 4.3 17.6 1.0 N A:HIS45 4.3 16.1 1.0 CG A:HIS47 4.3 23.8 1.0 ND1 A:HIS125 4.3 32.3 1.0 ND1 A:HIS70 4.4 22.8 1.0 O A:HIS45 4.6 16.6 1.0 C A:HIS45 4.6 16.4 1.0 O A:MET123 4.9 18.1 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