Calcium in PDB 3ctz: Structure of Human Cytosolic X-Prolyl Aminopeptidase

All present enzymatic activity of Structure of Human Cytosolic X-Prolyl Aminopeptidase:
3.4.11.9;

The structure of Structure of Human Cytosolic X-Prolyl Aminopeptidase, PDB code: 3ctz was solved by X.Li, Z.Lou, Z.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.62 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	71.444, 131.429, 169.076, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 19.6

The structure of Structure of Human Cytosolic X-Prolyl Aminopeptidase also contains other interesting chemical elements:

Manganese	(Mn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Calcium atom in the Structure of Human Cytosolic X-Prolyl Aminopeptidase (pdb code 3ctz). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Human Cytosolic X-Prolyl Aminopeptidase, PDB code: 3ctz:

Calcium binding site 1 out of 1 in the Structure of Human Cytosolic X-Prolyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Human Cytosolic X-Prolyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca626 b:18.1 occ:1.00 O A:THR435 2.4 16.3 1.0 O A:HOH739 2.5 21.0 1.0 O A:HOH717 2.5 19.8 1.0 O A:HOH670 2.5 17.4 1.0 OG1 A:THR435 2.6 17.0 1.0 C A:THR435 3.5 15.8 1.0 CB A:THR435 3.6 17.0 1.0 CA A:THR435 4.0 16.7 1.0 N A:THR435 4.2 17.0 1.0 O A:HOH887 4.4 30.7 1.0 OE2 A:GLU434 4.5 23.8 1.0 O A:HOH652 4.6 17.2 1.0 O A:HOH1155 4.6 43.8 1.0 O A:HOH946 4.6 33.6 1.0 OD1 A:ASP409 4.7 23.9 1.0 N A:PRO436 4.7 15.5 1.0 O A:HOH1154 4.7 38.8 1.0 CE1 A:HIS432 4.7 17.6 1.0 O A:LEU408 4.9 20.4 1.0 CG2 A:THR435 4.9 18.1 1.0

X.Li, Z.Lou, X.Li, W.Zhou, M.Ma, Y.Cao, Y.Geng, M.Bartlam, X.C.Zhang, Z.Rao. Structure of Human Cytosolic X-Prolyl Aminopeptidase: A Double Mn(II)-Dependent Dimeric Enzyme with A Novel Three-Domain Subunit J.Biol.Chem. V. 283 22858 2008.
ISSN: ISSN 0021-9258
PubMed: 18515364
DOI: 10.1074/JBC.M710274200