PDBsum entry 3hkn

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Lyase PDB id
Protein chain
257 a.a. *
GOL ×2
Waters ×92
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Human carbonic anhydrase ii in complex with (2,3,4,6-tetra-o beta-d-galactopyranosyl) -(1-4)-1,2,3,6-tetra-o-acetyl-1-th glucopyranosylsulfonamide
Structure: Carbonic anhydrase 2. Chain: a. Synonym: carbonic anhydrase ii, ca-ii, carbonate dehydratas carbonic anhydrasE C, cac. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2, carbonic anhydrase ii. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.80Å     R-factor:   0.198     R-free:   0.220
Authors: B.Paul,S.-A.Poulsen,A.Hofmann
Key ref: M.Lopez et al. (2009). S-glycosyl primary sulfonamides--a new structural class for selective inhibition of cancer-associated carbonic anhydrases. J Med Chem, 52, 6421-6432. PubMed id: 19827837
25-May-09     Release date:   13-Oct-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
260 a.a.
257 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    
J Med Chem 52:6421-6432 (2009)
PubMed id: 19827837  
S-glycosyl primary sulfonamides--a new structural class for selective inhibition of cancer-associated carbonic anhydrases.
M.Lopez, B.Paul, A.Hofmann, J.Morizzi, Q.K.Wu, S.A.Charman, A.Innocenti, D.Vullo, C.T.Supuran, S.A.Poulsen.
In this paper, we present a new class of carbonic anhydrase (CA) inhibitor that was designed to selectively target the extracellular domains of the cancer-relevant CA isozymes. The aromatic moiety of the classical zinc binding sulfonamide CA inhibitors is absent from these compounds and instead they incorporate a hydrophilic mono- or disaccharide fragment directly attached to the sulfonamide group to give S-glycosyl primary sulfonamides (1-10). The inhibition properties of these compounds at the physiologically abundant human CA isozymes I and II and cancer-associated IX and XII were determined, and all compounds had moderate potency with K(i)s in the micromolar range. We present the crystal structures of anomeric sulfonamides 4, 7, and 10 and the sugar sulfamate drug topiramate in complex with human recombinant CA II. From these structures, we have obtained valuable insights into ligand-protein interactions of these novel carbohydrate-based sulfonamides with CA.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20505865 V.Alterio, S.M.Monti, E.Truppo, C.Pedone, C.T.Supuran, and G.De Simone (2010).
The first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: the carbonic anhydrase I-topiramate complex.
  Org Biomol Chem, 8, 3528-3533.
PDB code: 3lxe
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