Zinc in PDB 2aps: Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae

The structure of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps was solved by K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.050, 123.880, 107.250, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 26.1

The structure of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae also contains other interesting chemical elements:

Copper

(Cu)

4 atoms

The binding sites of Zinc atom in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae (pdb code 2aps). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:30.1 occ:1.00 OD1 A:ASP106 2.0 27.3 1.0 ND1 A:HIS94 2.1 26.3 1.0 ND1 A:HIS85 2.1 37.6 1.0 ND1 A:HIS103 2.2 34.8 1.0 CG A:ASP106 2.8 25.9 1.0 CE1 A:HIS94 2.9 23.9 1.0 OD2 A:ASP106 2.9 25.2 1.0 CE1 A:HIS85 3.0 38.1 1.0 CE1 A:HIS103 3.1 34.9 1.0 CG A:HIS85 3.2 39.1 1.0 CG A:HIS103 3.2 34.4 1.0 CG A:HIS94 3.2 25.6 1.0 CB A:HIS103 3.5 32.2 1.0 CB A:HIS85 3.6 42.9 1.0 CB A:HIS94 3.7 27.2 1.0 CA A:HIS94 3.9 28.4 1.0 NE2 A:HIS94 4.1 21.2 1.0 NE2 A:HIS85 4.2 39.7 1.0 NE2 A:HIS103 4.2 33.3 1.0 CB A:ASP106 4.2 24.3 1.0 CD2 A:HIS94 4.3 23.4 1.0 CD2 A:HIS85 4.3 37.1 1.0 CD2 A:HIS103 4.3 32.2 1.0 CD1 A:LEU154 4.3 33.6 1.0 CD2 A:HIS60 4.7 34.7 1.0 CA A:ASP106 4.7 26.0 1.0 CA A:HIS103 4.8 33.0 1.0 N A:GLY95 4.8 26.3 1.0 N A:HIS103 4.9 32.5 1.0 N A:HIS94 4.9 31.9 1.0 C A:HIS94 4.9 25.4 1.0 N A:ASP106 4.9 29.9 1.0

Zinc binding site 2 out of 2 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn600 b:26.0 occ:1.00 OD1 B:ASP106 2.0 26.5 1.0 ND1 B:HIS103 2.0 22.5 1.0 ND1 B:HIS85 2.1 21.4 1.0 ND1 B:HIS94 2.1 25.9 1.0 CG B:ASP106 2.8 26.1 1.0 CE1 B:HIS103 2.9 23.9 1.0 OD2 B:ASP106 2.9 23.9 1.0 CE1 B:HIS94 3.0 26.5 1.0 CE1 B:HIS85 3.0 20.4 1.0 CG B:HIS103 3.1 21.6 1.0 CG B:HIS85 3.1 22.1 1.0 CG B:HIS94 3.2 28.0 1.0 CB B:HIS85 3.5 19.7 1.0 CB B:HIS103 3.6 24.5 1.0 CB B:HIS94 3.7 28.2 1.0 CA B:HIS94 3.8 28.4 1.0 NE2 B:HIS103 4.0 19.9 1.0 NE2 B:HIS85 4.1 20.6 1.0 NE2 B:HIS94 4.1 23.3 1.0 CD2 B:HIS103 4.2 22.9 1.0 CD2 B:HIS85 4.2 21.7 1.0 CB B:ASP106 4.3 22.6 1.0 CD2 B:HIS94 4.3 24.7 1.0 CD2 B:LEU154 4.4 25.0 1.0 CA B:HIS103 4.8 24.3 1.0 CA B:ASP106 4.8 24.6 1.0 N B:HIS103 4.8 26.0 1.0 N B:GLY95 4.8 25.6 1.0 N B:HIS94 4.8 27.7 1.0 CD2 B:HIS60 4.9 19.6 1.0 C B:HIS94 4.9 28.1 1.0 O B:GLN93 4.9 27.3 1.0 N B:ASP106 5.0 21.5 1.0

K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff. Cu,Zn Superoxide Dismutase Structure From A Microbial Pathogen Establishes A Class with A Conserved Dimer Interface. J.Mol.Biol. V. 296 145 2000.
ISSN: ISSN 0022-2836
PubMed: 10656823
DOI: 10.1006/JMBI.1999.3448