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PDBsum entry 2qoa

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protein ligands metals links
Lyase PDB id
2qoa
Jmol
Contents
Protein chain
257 a.a. *
Ligands
MBO
MAJ ×2
GOL
Metals
_ZN
_CL
Waters ×347
* Residue conservation analysis
PDB id:
2qoa
Name: Lyase
Title: Crystal structure of the complex of hcaii with an indane-sul inhibitor
Structure: Carbonic anhydrase 2. Chain: a. Synonym: carbonic anhydrase ii, carbonate dehydratase ii, c carbonic anhydrasE C. Ec: 4.2.1.1
Source: Homo sapiens. Human. Organism_taxid: 9606. Other_details: erythrocytes
Resolution:
1.60Å     R-factor:   0.177     R-free:   0.196
Authors: K.D'Ambrosio,G.De Simone
Key ref: K.D'Ambrosio et al. (2008). Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform II. ChemMedChem, 3, 473-477. PubMed id: 18161740
Date:
20-Jul-07     Release date:   22-Jan-08    
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   21 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
ChemMedChem 3:473-477 (2008)
PubMed id: 18161740  
 
 
Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform II.
K.D'Ambrosio, B.Masereel, A.Thiry, A.Scozzafava, C.T.Supuran, G.De Simone.
 
  ABSTRACT  
 
Indanesulfonamides are interesting lead compounds for designing selective inhibitors of the different isoforms of the zinc enzyme Carbonic Anhydrase (CA). Herein, we report for the first time the X-ray crystal structure of two such derivatives, namely indane-5-sulfonamide and indane-2-valproylamido-5-sulfonamide, in complex with the physiologically dominant human isoform II. The structural analysis reveals that, although these two inhibitors have quite similar chemical structures, the arrangement of their indane ring within the enzyme active site is significantly diverse. Thus, our findings suggest that the introduction of bulky substituents on the indane-sulfonamide ring may alter the binding mode of this potent class of CA inhibitors, although retaining good inhibitory properties. Accordingly, the introduction of bulky tail moieties on the indane-sulfonamide scaffold may represent a powerful strategy to induce a desired physicochemical property to an aromatic sulfonamide or to obtain inhibitors with diverse inhibition profiles and selectivity for various mammalian CAs.