Zinc in PDB 4fru: Crystal Structure of Horse Wild-Type Cyclophilin B

All present enzymatic activity of Crystal Structure of Horse Wild-Type Cyclophilin B:
5.2.1.8;

The structure of Crystal Structure of Horse Wild-Type Cyclophilin B, PDB code: 4fru was solved by S.P.Boudko, Y.Ishikawa, H.P.Bachinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.42 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.880, 44.070, 60.570, 90.00, 95.20, 90.00
R / Rfree (%)	11.6 / 13.9

The binding sites of Zinc atom in the Crystal Structure of Horse Wild-Type Cyclophilin B (pdb code 4fru). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Horse Wild-Type Cyclophilin B, PDB code: 4fru:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Horse Wild-Type Cyclophilin B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Horse Wild-Type Cyclophilin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:9.9 occ:0.82 O A:HOH472 2.0 17.4 1.0 NE2 A:HIS133 2.0 7.0 1.0 O A:HOH476 2.2 17.4 1.0 CE1 A:HIS133 2.9 6.1 1.0 HE1 A:HIS133 3.0 7.3 1.0 CD2 A:HIS133 3.1 6.3 1.0 HD2 A:HIS133 3.3 7.6 1.0 HD22 A:LEU129 3.8 12.8 1.0 OD1 A:ASN109 3.9 6.4 1.0 HB3 A:LYS132 4.0 10.0 0.7 ND1 A:HIS133 4.1 5.4 1.0 HB3 A:LYS132 4.1 8.8 0.3 CG A:HIS133 4.2 5.1 1.0 HD22 A:ASN109 4.3 5.9 1.0 HB2 A:LYS132 4.4 8.8 0.3 HD2 A:LYS132 4.5 10.7 0.3 CD2 A:LEU129 4.6 10.6 1.0 CG A:ASN109 4.6 5.5 1.0 HB2 A:LYS132 4.6 10.0 0.7 HD23 A:LEU129 4.7 12.8 1.0 HD3 A:LYS132 4.7 18.8 0.7 HD21 A:LEU129 4.7 12.8 1.0 CB A:LYS132 4.7 7.4 0.3 CB A:LYS132 4.8 8.3 0.7 O A:ASN109 4.8 8.2 1.0 ND2 A:ASN109 4.8 4.9 1.0 HD1 A:HIS133 4.8 6.5 1.0 HD3 A:LYS132 4.9 10.7 0.3

Zinc binding site 2 out of 2 in the Crystal Structure of Horse Wild-Type Cyclophilin B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Horse Wild-Type Cyclophilin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:5.1 occ:0.97 OD2 A:ASP21 1.9 5.2 1.0 O A:HOH320 2.0 6.7 1.0 CG A:ASP21 2.8 4.1 1.0 OD1 A:ASP21 3.1 4.5 1.0 H51 A:ME2203 3.7 18.1 1.0 CB A:ASP21 4.2 4.8 1.0 H61 A:ME2203 4.3 19.5 1.0 HB3 A:ASP21 4.4 5.7 1.0 HB2 A:ASP21 4.4 5.7 1.0 C5 A:ME2203 4.6 15.1 1.0

S.P.Boudko, Y.Ishikawa, T.F.Lerch, J.Nix, M.S.Chapman, H.P.Bachinger. Crystal Structures of Wild-Type and Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse. Bmc Res Notes V. 5 626 2012.
ISSN: ESSN 1756-0500
PubMed: 23137129
DOI: 10.1186/1756-0500-5-626