Copper in PDB 1cb4: Crystal Structure of Copper, Zinc Superoxide Dismutase

All present enzymatic activity of Crystal Structure of Copper, Zinc Superoxide Dismutase:
1.15.1.1;

The structure of Crystal Structure of Copper, Zinc Superoxide Dismutase, PDB code: 1cb4 was solved by M.A.Hough, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	105.100, 199.180, 51.300, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.8

The structure of Crystal Structure of Copper, Zinc Superoxide Dismutase also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Copper atom in the Crystal Structure of Copper, Zinc Superoxide Dismutase (pdb code 1cb4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Copper, Zinc Superoxide Dismutase, PDB code: 1cb4:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu152 b:38.8 occ:1.00 ND1 A:HIS44 1.8 32.6 1.0 CE1 A:HIS118 2.1 24.3 1.0 O A:HOH158 2.2 39.6 1.0 CE1 A:HIS46 2.2 20.1 1.0 NE2 A:HIS61 2.4 35.9 1.0 CE1 A:HIS44 2.8 32.6 1.0 CG A:HIS44 2.8 31.1 1.0 NE2 A:HIS118 2.9 23.6 1.0 NE2 A:HIS46 3.0 20.0 1.0 ND1 A:HIS118 3.0 23.0 1.0 CD2 A:HIS61 3.0 35.2 1.0 CB A:HIS44 3.2 28.2 1.0 ND1 A:HIS46 3.3 17.5 1.0 CE1 A:HIS61 3.5 35.9 1.0 NE2 A:HIS44 3.8 32.8 1.0 CD2 A:HIS44 3.9 30.5 1.0 CD2 A:HIS118 4.1 24.0 1.0 CG A:HIS118 4.1 25.6 1.0 CD2 A:HIS46 4.2 19.5 1.0 CG A:HIS61 4.3 33.7 1.0 CG A:HIS46 4.4 18.8 1.0 ND1 A:HIS61 4.5 35.4 1.0 CG1 A:VAL116 4.5 25.9 1.0 CA A:HIS44 4.5 25.4 1.0 CB A:VAL116 4.6 26.8 1.0 N A:HIS44 4.7 26.5 1.0

Copper binding site 2 out of 3 in the Crystal Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu153 b:28.1 occ:1.00 OD1 A:ASP81 1.8 21.9 1.0 ND1 A:HIS78 1.8 23.4 1.0 ND1 A:HIS61 2.0 35.4 1.0 ND1 A:HIS69 2.3 33.4 1.0 CE1 A:HIS78 2.6 23.5 1.0 CG A:ASP81 2.7 26.5 1.0 CG A:HIS78 2.9 24.6 1.0 CE1 A:HIS61 2.9 35.9 1.0 OD2 A:ASP81 3.0 25.6 1.0 CG A:HIS61 3.0 33.7 1.0 CE1 A:HIS69 3.1 34.3 1.0 CG A:HIS69 3.3 33.6 1.0 CB A:HIS61 3.4 30.4 1.0 CB A:HIS78 3.5 25.7 1.0 CB A:HIS69 3.6 32.8 1.0 NE2 A:HIS78 3.8 22.7 1.0 CA A:HIS69 3.8 34.3 1.0 O A:LYS134 3.9 38.2 1.0 CD2 A:HIS78 3.9 24.1 1.0 NE2 A:HIS61 4.1 35.9 1.0 CD2 A:HIS61 4.1 35.2 1.0 CB A:ASP81 4.1 27.0 1.0 NE2 A:HIS69 4.3 37.4 1.0 CD2 A:HIS69 4.4 35.1 1.0 CA A:ASP81 4.6 27.4 1.0 O A:HOH159 4.7 33.9 1.0 N A:GLY70 4.8 33.8 1.0 CA A:HIS78 4.8 26.5 1.0 N A:HIS78 4.8 31.3 1.0 C A:HIS69 4.8 34.5 1.0 N A:ASP81 4.9 27.9 1.0 N A:HIS69 4.9 35.5 1.0 CA A:HIS61 5.0 27.9 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu152 b:17.0 occ:1.00 ND1 B:HIS44 2.0 11.9 1.0 CE1 B:HIS46 2.1 7.5 1.0 NE2 B:HIS118 2.1 8.0 1.0 NE2 B:HIS61 2.2 11.1 1.0 O B:HOH164 2.4 16.2 1.0 NE2 B:HIS46 2.7 6.6 1.0 CD2 B:HIS61 2.9 10.6 1.0 CG B:HIS44 2.9 8.4 1.0 CE1 B:HIS118 2.9 5.2 1.0 CE1 B:HIS44 3.0 11.4 1.0 CD2 B:HIS118 3.1 6.5 1.0 CB B:HIS44 3.2 5.5 1.0 CE1 B:HIS61 3.3 11.6 1.0 ND1 B:HIS46 3.3 9.8 1.0 CD2 B:HIS46 4.0 5.4 1.0 ND1 B:HIS118 4.1 8.3 1.0 CD2 B:HIS44 4.1 9.7 1.0 NE2 B:HIS44 4.1 11.9 1.0 CG B:HIS61 4.1 11.1 1.0 CG B:HIS118 4.2 6.1 1.0 CG B:HIS46 4.3 7.1 1.0 ND1 B:HIS61 4.3 9.4 1.0 CA B:HIS44 4.6 6.0 1.0 CG1 B:VAL116 4.6 7.0 1.0 CB B:VAL116 4.7 9.2 1.0 N B:HIS44 4.7 3.9 1.0 O B:HOH181 4.9 13.2 1.0

M.A.Hough, S.S.Hasnain. Crystallographic Structures of Bovine Copper-Zinc Superoxide Dismutase Reveal Asymmetry in Two Subunits: Functionally Important Three and Five Coordinate Copper Sites Captured in the Same Crystal. J.Mol.Biol. V. 287 579 1999.
ISSN: ISSN 0022-2836
PubMed: 10092461
DOI: 10.1006/JMBI.1999.2610