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PDBsum entry 3r16

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protein ligands metals links
Lyase PDB id
3r16
Jmol
Contents
Protein chain
257 a.a.
Ligands
GOL ×2
5UN
DMS
Metals
_ZN
Waters ×327
PDB id:
3r16
Name: Lyase
Title: Human caii bound to n-(4-sulfamoylphenyl)-2-(thiophen-2-yl)
Structure: Carbonic anhydrase 2. Chain: a. 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: 562
Resolution:
1.60Å     R-factor:   0.152     R-free:   0.173
Authors: S.Biswas,R.Mckenna,C.T.Supuran
Key ref: S.Biswas et al. (2011). Conformational variability of different sulfonamide inhibitors with thienyl-acetamido moieties attributes to differential binding in the active site of cytosolic human carbonic anhydrase isoforms. Bioorg Med Chem, 19, 3732-3738. PubMed id: 21620713
Date:
09-Mar-11     Release date:   25-May-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
257 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: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   11 terms 
  Biological process     angiotensin-mediated signaling pathway   22 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
Bioorg Med Chem 19:3732-3738 (2011)
PubMed id: 21620713  
 
 
Conformational variability of different sulfonamide inhibitors with thienyl-acetamido moieties attributes to differential binding in the active site of cytosolic human carbonic anhydrase isoforms.
S.Biswas, M.Aggarwal, ..Güzel, A.Scozzafava, R.McKenna, C.T.Supuran.
 
  ABSTRACT  
 
No abstract given.