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Zinc in PDB 2o3e: Crystal Structure of Engineered Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site.

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

All present enzymatic activity of Crystal Structure of Engineered Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site.:
3.4.24.16;

Protein crystallography data

The structure of Crystal Structure of Engineered Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site., PDB code: 2o3e 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) 43.85 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 159.550, 87.700, 58.400, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 26.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Engineered Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site. (pdb code 2o3e). 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 Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site., PDB code: 2o3e:

Zinc binding site 1 out of 1 in 2o3e

Go back to Zinc Binding Sites List in 2o3e
Zinc binding site 1 out of 1 in the Crystal Structure of Engineered Neurolysin with Thimet Oligopeptidase Specificity For 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 Neurolysin with Thimet Oligopeptidase Specificity For Neurotensin Cleavage Site. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn679

b:30.4
occ:1.00
 NE2 A:HIS478 2.2 27.7 1.0
OE1 A:GLU503 2.2 23.9 1.0
NE2 A:HIS474 2.2 22.3 1.0
O A:HOH888 2.3 26.9 1.0
OE2 A:GLU503 2.7 25.9 1.0
CD A:GLU503 2.7 23.2 1.0
CD2 A:HIS478 3.1 23.9 1.0
CE1 A:HIS474 3.1 23.8 1.0
CE1 A:HIS478 3.2 23.6 1.0
CD2 A:HIS474 3.3 23.4 1.0
OG A:SER506 3.7 24.3 1.0
CB A:SER506 4.1 26.8 1.0
CG A:GLU503 4.2 24.1 1.0
O A:HOH695 4.2 32.2 1.0
ND1 A:HIS474 4.2 23.5 1.0
CG A:HIS478 4.3 23.1 1.0
ND1 A:HIS478 4.3 22.7 1.0
CG A:HIS474 4.4 25.1 1.0
OE2 A:GLU475 4.4 35.4 1.0
OE1 A:GLU475 4.9 37.4 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

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