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PDBsum entry 3s77

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protein ligands metals links
Lyase PDB id
3s77
Jmol
Contents
Protein chain
258 a.a.
Ligands
EVI ×2
Metals
_ZN
Waters ×113
PDB id:
3s77
Name: Lyase
Title: The origin of the hydrophobic effect in the molecular recogn arylsulfonamides by carbonic anhydrase
Structure: Carbonic anhydrase 2. Chain: b. Synonym: carbonate dehydratase ii, carbonic anhydrasE C, ca carbonic anhydrase ii, ca-ii. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.86Å     R-factor:   0.180     R-free:   0.219
Authors: P.W.Snyder,A.Heroux,G.W.Whitesides
Key ref: P.W.Snyder et al. (2011). Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase. Proc Natl Acad Sci U S A, 108, 17889-17894. PubMed id: 22011572 DOI: 10.1073/pnas.1114107108
Date:
26-May-11     Release date:   19-Oct-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
258 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 space   10 terms 
  Biological process     angiotensin-mediated signaling pathway   20 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
DOI no: 10.1073/pnas.1114107108 Proc Natl Acad Sci U S A 108:17889-17894 (2011)
PubMed id: 22011572  
 
 
Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase.
P.W.Snyder, J.Mecinovic, D.T.Moustakas, S.W.Thomas, M.Harder, E.T.Mack, M.R.Lockett, A.Héroux, W.Sherman, G.M.Whitesides.
 
  ABSTRACT  
 
No abstract given.