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PDBsum entry 1bim

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protein ligands Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
1bim
Jmol
Contents
Protein chain
334 a.a. *
Ligands
0QB ×2
* Residue conservation analysis
PDB id:
1bim
Name: Hydrolase/hydrolase inhibitor
Title: Crystallographic studies on the binding modes of p2-p3 butan renin inhibitors
Structure: Renin. Chain: a, b. Synonym: angiotensinogenase. Engineered: yes. Other_details: glycosylated
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cmv ie-human preprorenin cdna, ren. Expressed in: canis lupus familiaris. Expression_system_taxid: 9615. Other_details: stably transferred
Biol. unit: Hexamer (from PQS)
Resolution:
2.80Å     R-factor:   0.178    
Authors: L.Tong
Key ref: L.Tong et al. (1995). Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors. J Biol Chem, 270, 29520-29524. PubMed id: 7493993
Date:
27-Sep-95     Release date:   29-Jan-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00797  (RENI_HUMAN) -  Renin
Seq:
Struc:
406 a.a.
334 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.23.15  - Renin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleaves Leu-|- bond in angiotensinogen to generate angiotensin I.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     aspartic-type endopeptidase activity     1 term  

 

 
J Biol Chem 270:29520-29524 (1995)
PubMed id: 7493993  
 
 
Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors.
L.Tong, S.Pav, D.Lamarre, B.Simoneau, P.Lavallée, G.Jung.
 
  ABSTRACT  
 
The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20101644 V.Zoete, A.Grosdidier, M.Cuendet, and O.Michielin (2010).
Use of the FACTS solvation model for protein-ligand docking calculations. Application to EADock.
  J Mol Recognit, 23, 457-461.  
11714911 N.S.Andreeva, and L.D.Rumsh (2001).
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
  Protein Sci, 10, 2439-2450.  
9265722 T.Kieber-Emmons, R.Murali, and M.I.Greene (1997).
Therapeutic peptides and peptidomimetics.
  Curr Opin Biotechnol, 8, 435-441.  
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