Zinc in PDB 4frv: Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse

All present enzymatic activity of Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse:
5.2.1.8;

The structure of Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse, PDB code: 4frv 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)	16.29 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.790, 44.160, 60.110, 90.00, 95.45, 90.00
R / Rfree (%)	11.9 / 13.8

The binding sites of Zinc atom in the Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse (pdb code 4frv). 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 Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse, PDB code: 4frv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse


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 Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:5.9 occ:0.87 O A:HOH479 2.0 10.0 1.0 NE2 A:HIS133 2.0 5.3 1.0 O A:HOH481 2.1 10.7 1.0 CE1 A:HIS133 2.9 4.6 1.0 HE1 A:HIS133 3.0 5.6 1.0 CD2 A:HIS133 3.1 5.0 1.0 HD2 A:HIS133 3.3 6.0 1.0 HD22 A:LEU129 3.6 8.5 1.0 OD1 A:ASN109 3.8 5.4 1.0 HB3 A:LYS132 3.9 7.7 0.7 HB3 A:LYS132 4.0 9.9 0.3 ND1 A:HIS133 4.1 4.3 1.0 O A:HOH470 4.1 23.4 1.0 CG A:HIS133 4.2 4.3 1.0 HD22 A:ASN109 4.3 5.5 1.0 O A:HOH567 4.3 27.8 1.0 CD2 A:LEU129 4.4 7.1 1.0 HD23 A:LEU129 4.4 8.5 1.0 HD3 A:LYS132 4.4 13.8 0.7 HB2 A:LYS132 4.5 9.9 0.3 HD21 A:LEU129 4.5 8.5 1.0 CG A:ASN109 4.6 4.8 1.0 HB2 A:LYS132 4.6 7.7 0.7 HD3 A:LYS132 4.6 16.2 0.3 CB A:LYS132 4.7 6.4 0.7 O A:ASN109 4.7 6.9 1.0 CB A:LYS132 4.7 8.2 0.3 ND2 A:ASN109 4.7 4.6 1.0 HD1 A:HIS133 4.8 5.1 1.0 HD2 A:LYS132 4.9 16.2 0.3 H A:GLY111 5.0 8.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse


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 Mutated Cyclophilin B That Causes Hyperelastosis Cutis in the American Quarter Horse within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:6.0 occ:1.00 OD2 A:ASP21 1.9 6.5 1.0 O A:HOH307 2.0 8.2 1.0 CG A:ASP21 2.9 5.1 1.0 OD1 A:ASP21 3.1 6.0 1.0 H51 A:ME2203 3.6 16.8 1.0 CB A:ASP21 4.2 5.3 1.0 HB3 A:ASP21 4.4 6.4 1.0 HB2 A:ASP21 4.5 6.4 1.0 C5 A:ME2203 4.6 14.0 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