Zinc in PDB 3ici: Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment

All present enzymatic activity of Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment:
5.2.1.8;

The structure of Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment, PDB code: 3ici was solved by G.Kozlov, K.Gehring, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.411, 44.295, 55.427, 89.94, 94.46, 114.03
R / Rfree (%)	18.8 / 23.9

The binding sites of Zinc atom in the Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment (pdb code 3ici). 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 Cyclophilin B in Complex with Calmegin Fragment, PDB code: 3ici:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment


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 Cyclophilin B in Complex with Calmegin Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:17.0 occ:1.00 OD2 A:ASP2 1.9 22.2 1.0 O A:GLY-3 2.4 20.9 1.0 CG A:ASP2 2.7 28.2 1.0 CA A:GLY-3 2.8 21.6 1.0 C A:GLY-3 2.9 21.2 1.0 OD1 A:ASP2 2.9 25.5 1.0 CB A:ASP2 4.1 29.3 1.0 N A:PRO-2 4.2 21.1 1.0 N A:GLY-3 4.2 22.7 1.0 O A:HOH953 4.4 35.6 1.0 O A:PRO-2 4.4 20.7 1.0 CD2 A:LEU-1 4.6 18.6 1.0 C A:PRO-2 4.6 21.0 1.0 CA A:PRO-2 4.9 21.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cyclophilin B in Complex with Calmegin Fragment


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 Cyclophilin B in Complex with Calmegin Fragment within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:16.1 occ:1.00 OD2 B:ASP2 2.0 18.2 1.0 O B:GLY-3 2.3 20.0 1.0 O B:HOH501 2.3 13.7 1.0 CA B:GLY-3 2.8 20.7 1.0 CG B:ASP2 2.8 24.9 1.0 C B:GLY-3 2.8 20.3 1.0 OD1 B:ASP2 2.9 22.3 1.0 O B:HOH675 4.1 32.1 1.0 N B:PRO-2 4.1 20.0 1.0 N B:GLY-3 4.2 22.1 1.0 CB B:ASP2 4.2 26.3 1.0 O B:HOH663 4.5 23.4 1.0 O B:HOH567 4.5 12.7 1.0 O B:PRO-2 4.5 18.8 1.0 O B:HOH951 4.6 36.4 1.0 CD2 B:LEU-1 4.6 18.8 1.0 C B:PRO-2 4.6 19.5 1.0 CA B:PRO-2 4.9 19.9 1.0

G.Kozlov, S.Bastos-Aristizabal, P.Maattanen, A.Rosenauer, F.Zheng, A.Killikelly, J.F.Trempe, D.Y.Thomas, K.Gehring. Structural Basis of Cyclophilin B Binding By the Calnexin/Calreticulin P-Domain. J.Biol.Chem. V. 285 35551 2010.
ISSN: ISSN 0021-9258
PubMed: 20801878
DOI: 10.1074/JBC.M110.160101