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PDBsum entry 3nxq

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3nxq
Jmol
Contents
Protein chain
607 a.a. *
Ligands
RX4 ×2
NAG-FUC ×2
NAG-NAG ×2
NAG-NAG-BMA-FUC ×2
P6G ×2
PEG ×2
PG4 ×2
Metals
_ZN ×2
_CL ×2
Waters ×563
* Residue conservation analysis
PDB id:
3nxq
Name: Hydrolase/hydrolase inhibitor
Title: Angiotensin converting enzyme n domain glycsoylation mutant in complex with rxp407
Structure: Angiotensin-converting enzyme. Chain: a, b. Fragment: n domain (unp residues 30-657). Synonym: ace, dipeptidyl carboxypeptidase i, kininase ii, angiotensin-converting enzyme, soluble form. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ace, dcp, dcp1. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: ovary cells
Resolution:
1.99Å     R-factor:   0.194     R-free:   0.237
Authors: C.S.Anthony,H.R.Corradi,S.L.U.Schwager,P.Redelinghuys,D.Geor V.Dive,K.R.Acharya,E.D.Sturrock
Date:
14-Jul-10     Release date:   08-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P12821  (ACE_HUMAN) -  Angiotensin-converting enzyme
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1306 a.a.
607 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 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