Atomistry » Zinc » PDB 2nwp-2o6i » 2o36
Atomistry »
  Zinc »
    PDB 2nwp-2o6i »
      2o36 »

Zinc in PDB 2o36: Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site

Enzymatic activity of Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site

All present enzymatic activity of Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site:
3.4.24.15;

Protein crystallography data

The structure of Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site, PDB code: 2o36 was solved by D.W.Rodgers, E.J.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.72 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.120, 99.250, 105.710, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site (pdb code 2o36). 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 Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site, PDB code: 2o36:

Zinc binding site 1 out of 1 in 2o36

Go back to Zinc Binding Sites List in 2o36
Zinc binding site 1 out of 1 in the Crystal Structure of Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site


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 Engineered Thimet Oligopeptidase with Neurolysin Specificity in Neurotensin Cleavage Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn690

b:22.5
occ:1.00
 OE1 A:GLU502 2.0 15.8 1.0
O A:HOH1161 2.1 29.8 1.0
NE2 A:HIS477 2.2 16.0 1.0
NE2 A:HIS473 2.2 17.2 1.0
CD A:GLU502 2.8 18.6 1.0
OE2 A:GLU502 3.0 19.8 1.0
CD2 A:HIS477 3.1 17.0 1.0
CD2 A:HIS473 3.1 17.7 1.0
CE1 A:HIS477 3.2 14.3 1.0
CE1 A:HIS473 3.2 20.6 1.0
OE1 A:GLU474 4.1 26.9 1.0
CG A:HIS477 4.2 14.1 1.0
ND1 A:HIS477 4.3 14.8 1.0
CG A:HIS473 4.3 16.8 1.0
CG A:GLU502 4.3 14.6 1.0
ND1 A:HIS473 4.3 17.0 1.0
O A:HOH759 4.4 19.6 1.0
OE2 A:GLU474 4.5 24.6 1.0
CD A:GLU474 4.6 22.7 1.0
CB A:SER505 4.6 14.2 1.0
OG A:SER505 4.7 15.8 1.0
CB A:GLU502 4.9 14.3 1.0
CA A:GLU502 5.0 15.5 1.0

Reference:

E.J.Lim, S.Sampath, J.Coll-Rodriguez, J.Schmidt, K.Ray, D.W.Rodgers. Swapping the Substrate Specificities of the Neuropeptidases Neurolysin and Thimet Oligopeptidase. J.Biol.Chem. V. 282 9722 2007.
ISSN: ISSN 0021-9258
PubMed: 17251185
DOI: 10.1074/JBC.M609897200
Page generated: Thu Oct 17 02:26:09 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy