PDBsum entry 1eou

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protein ligands metals links
Lyase PDB id
Protein chain
258 a.a. *
Waters ×179
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of human carbonic anhydrase ii complexed with an anticonvulsant sugar sulfamate
Structure: Carbonic anhydrase ii (ca ii). Chain: a. Ec:
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: erythrocytes. Cellular_location: cytoplasmerythrocytes
2.10Å     R-factor:   0.176     R-free:   0.229
Authors: R.Recacha,M.J.Costanzo,B.E.Maryanoff,D.Chattopadhyay
Key ref: R.Recacha et al. (2002). Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate. Biochem J, 361, 437-441. PubMed id: 11802772
24-Mar-00     Release date:   13-Feb-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
260 a.a.
258 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
= 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    
Biochem J 361:437-441 (2002)
PubMed id: 11802772  
Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate.
R.Recacha, M.J.Costanzo, B.E.Maryanoff, D.Chattopadhyay.
The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19058143 J.Y.Winum, S.A.Poulsen, and C.T.Supuran (2009).
Therapeutic applications of glycosidic carbonic anhydrase inhibitors.
  Med Res Rev, 29, 419-435.  
18335973 V.M.Krishnamurthy, G.K.Kaufman, A.R.Urbach, I.Gitlin, K.L.Gudiksen, D.B.Weibel, and G.M.Whitesides (2008).
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
  Chem Rev, 108, 946.  
15478125 J.Y.Winum, A.Scozzafava, J.L.Montero, and C.T.Supuran (2005).
Sulfamates and their therapeutic potential.
  Med Res Rev, 25, 186-228.  
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