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PDBsum entry 4asr

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protein ligands metals links
Hydrolase PDB id
4asr
Jmol
Contents
Protein chain
598 a.a.
Ligands
ARG-PRO-PRO-GLY
NAG-NAG-MAN-BMA-
MAN-BMA
NAG ×2
FLC
Metals
_ZN
Waters ×573
PDB id:
4asr
Name: Hydrolase
Title: Crystal structure of ance in complex with thr6-bradykinin
Structure: Angiotensin-converting enzyme. Chain: a. Fragment: residues 17-614. Synonym: dipeptidyl carboxypeptidase i, kininase ii. Engineered: yes. Bradykinin. Chain: p. Synonym: thr6-bradykinin. Mutation: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: komagataella pastoris. Expression_system_taxid: 644223. Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606
Resolution:
1.90Å     R-factor:   0.183     R-free:   0.199
Authors: M.Akif,G.Masuyer,E.D.Sturrock,R.E.Isaac,K.R.Acharya
Key ref: M.Akif et al. (2012). Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. FEBS J, 279, 4525-4534. PubMed id: 23082758
Date:
02-May-12     Release date:   31-Oct-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q10714  (ACE_DROME) -  Angiotensin-converting enzyme
Seq:
Struc:
 
Seq:
Struc:
615 a.a.
598 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.15.1  - Peptidyl-dipeptidase A.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Xbb, when Xaa is not Pro, and Xbb is neither Asp nor Glu. Converts angiotensin I to angiotensin II.
      Cofactor: Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     proteolysis   1 term 
  Biochemical function     metallopeptidase activity     2 terms  

 

 
FEBS J 279:4525-4534 (2012)
PubMed id: 23082758  
 
 
Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster.
M.Akif, G.Masuyer, R.J.Bingham, E.D.Sturrock, R.E.Isaac, K.R.Acharya.
 
  ABSTRACT  
 
No abstract given.