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Zinc in PDB 4p10: Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid

Enzymatic activity of Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid

All present enzymatic activity of Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid:
3.4.17.20;

Protein crystallography data

The structure of Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid, PDB code: 4p10 was solved by K.Hallberg, T.Sjogren, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 94.91 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.576, 49.243, 95.048, 90.00, 93.12, 90.00
R / Rfree (%) 18.4 / 21.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid (pdb code 4p10). 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 Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid, PDB code: 4p10:

Zinc binding site 1 out of 1 in 4p10

Go back to Zinc Binding Sites List in 4p10
Zinc binding site 1 out of 1 in the Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Pro-Carboxypeptidase U in Complex with 5-(3-Aminopropyl)-1-Propyl-6,7- Dihydro-4H-Benzimidazole-5-Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:20.5
occ:1.00
 ND1 A:HIS181 1.8 19.2 1.0
N6 A:2B8501 2.0 20.1 1.0
OE1 A:GLU184 2.2 16.2 1.0
ND1 A:HIS310 2.2 20.1 1.0
OE2 A:GLU184 2.5 15.8 1.0
CD A:GLU184 2.7 14.6 1.0
CE1 A:HIS181 2.7 21.4 1.0
CG A:HIS181 2.9 16.1 1.0
C5 A:2B8501 2.9 18.7 1.0
C7 A:2B8501 3.1 18.8 1.0
CG A:HIS310 3.1 16.0 1.0
CB A:HIS310 3.3 17.0 1.0
CE1 A:HIS310 3.3 19.3 1.0
CB A:HIS181 3.3 16.0 1.0
C8 A:2B8501 3.5 19.0 1.0
NE2 A:HIS181 3.8 17.7 1.0
CD2 A:HIS181 3.9 16.7 1.0
O A:HOH645 4.0 16.4 1.0
N4 A:2B8501 4.1 19.7 1.0
CG A:GLU184 4.1 15.1 1.0
CA A:HIS310 4.2 16.6 1.0
C16 A:2B8501 4.2 18.0 1.0
O A:SER311 4.2 18.2 1.0
CD2 A:HIS310 4.3 16.7 1.0
NE2 A:HIS310 4.3 16.7 1.0
N A:SER311 4.5 17.7 1.0
O A:HOH666 4.7 22.1 1.0
CA A:HIS181 4.7 16.5 1.0
NH1 A:ARG239 4.8 34.6 1.0
N A:HIS181 4.9 16.6 1.0
O19 A:2B8501 4.9 19.7 1.0
C A:HIS310 4.9 17.6 1.0
CB A:GLU184 4.9 15.7 1.0
C9 A:2B8501 5.0 18.4 1.0

Reference:

M.Brink, A.Dahlen, T.Olsson, M.Polla, T.Svensson. Design and Synthesis of Conformationally Restricted Inhibitors of Active Thrombin Activatable Fibrinolysis Inhibitor (Tafia). Bioorg.Med.Chem. V. 22 2261 2014.
ISSN: ESSN 1464-3391
PubMed: 24588961
DOI: 10.1016/J.BMC.2014.02.010
Page generated: Sun Oct 27 04:08:12 2024

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