Zinc in PDB 1s4b: Crystal Structure of Human Thimet Oligopeptidase.

All present enzymatic activity of Crystal Structure of Human Thimet Oligopeptidase.:
3.4.24.15;

The structure of Crystal Structure of Human Thimet Oligopeptidase., PDB code: 1s4b was solved by K.Ray, C.S.Hines, J.Coll-Rodriguez, D.W.Rodgers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	77.167, 99.104, 105.505, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 23.3

The binding sites of Zinc atom in the Crystal Structure of Human Thimet Oligopeptidase. (pdb code 1s4b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Thimet Oligopeptidase., PDB code: 1s4b:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Thimet Oligopeptidase.


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 Human Thimet Oligopeptidase. within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn1 b:17.4 occ:1.00 OE1 P:GLU502 2.0 14.9 1.0 O P:HOH1163 2.1 23.0 1.0 NE2 P:HIS477 2.1 14.0 1.0 NE2 P:HIS473 2.2 13.2 1.0 CD P:GLU502 2.8 17.7 1.0 OE2 P:GLU502 2.9 19.7 1.0 CD2 P:HIS477 3.0 15.2 1.0 CD2 P:HIS473 3.1 13.4 1.0 CE1 P:HIS473 3.1 15.5 1.0 CE1 P:HIS477 3.2 14.7 1.0 CG P:HIS477 4.2 15.7 1.0 CG P:GLU502 4.2 14.3 1.0 OE2 P:GLU474 4.2 28.8 1.0 ND1 P:HIS477 4.2 14.7 1.0 ND1 P:HIS473 4.2 15.3 1.0 CG P:HIS473 4.3 13.6 1.0 OE1 P:GLU474 4.4 29.1 1.0 CB P:SER505 4.5 11.7 1.0 OG P:SER505 4.6 14.9 1.0 O P:HOH733 4.7 17.5 1.0 CD P:GLU474 4.7 26.4 1.0 CB P:GLU502 4.7 12.2 1.0 CA P:GLU502 4.8 12.8 1.0

K.Ray, C.S.Hines, J.Coll-Rodriguez, D.W.Rodgers. Crystal Structure of Human Thimet Oligopeptidase Provides Insight Into Substrate Recognition, Regulation, and Localization J.Biol.Chem. V. 279 20480 2004.
ISSN: ISSN 0021-9258
PubMed: 14998993
DOI: 10.1074/JBC.M400795200