spacer
spacer

PDBsum entry 3fe4

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3fe4
Jmol
Contents
Protein chain
244 a.a. *
Ligands
GOL ×2
Metals
_MG ×2
Waters ×429
* Residue conservation analysis
PDB id:
3fe4
Name: Lyase
Title: Crystal structure of human carbonic anhydrase vi
Structure: Carbonic anhydrase 6. Chain: a, b. Fragment: carbonic anhydrase vi, unp residues 21-290. Synonym: carbonic anhydrase vi, ca-vi, carbonate dehydratas secreted carbonic anhydrase, salivary carbonic anhydrase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca6. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.179     R-free:   0.235
Authors: E.S.Pilka,G.Kochan,E.Krysztofinska,J.Muniz,W.W.Yue,A.K.Roos, Delft,C.H.Arrowsmith,J.Weigelt,A.Edwards,C.Bountra,U.Opperm Structural Genomics Consortium (Sgc)
Key ref: E.S.Pilka et al. (2012). Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development. Biochem Biophys Res Commun, 419, 485-489. PubMed id: 22366092
Date:
27-Nov-08     Release date:   16-Dec-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23280  (CAH6_HUMAN) -  Carbonic anhydrase 6
Seq:
Struc:
308 a.a.
244 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
H(2)CO(3)
= CO(2)
+ H(2)O
      Cofactor: Zinc
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   4 terms 
  Biological process     small molecule metabolic process   4 terms 
  Biochemical function     lyase activity     4 terms  

 

 
    Added reference    
 
 
Biochem Biophys Res Commun 419:485-489 (2012)
PubMed id: 22366092  
 
 
Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.
E.S.Pilka, G.Kochan, U.Oppermann, W.W.Yue.
 
  ABSTRACT  
 
Zn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9Å crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors.