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PDBsum entry 3fw3

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3fw3
Jmol
Contents
Protein chain
249 a.a. *
Ligands
ETS ×2
GLC
SO4 ×2
Metals
_ZN ×2
Waters ×264
* Residue conservation analysis
PDB id:
3fw3
Name: Lyase
Title: Crystal structure of soluble domain of ca4 in complex with d
Structure: Carbonic anhydrase 4. Chain: a, b. Fragment: soluble domain. Synonym: carbonic anhydrase iv, ca-iv, carbonate dehydratas engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca4. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.72Å     R-factor:   0.177     R-free:   0.206
Authors: S.E.Greasley,R.A.A.Ferre,R.Paz,J.Wickersham
Key ref: W.Vernier et al. (2010). Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation. Bioorg Med Chem, 18, 3307-3319. PubMed id: 20363633 DOI: 10.1016/j.bmc.2010.03.014
Date:
16-Jan-09     Release date:   01-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22748  (CAH4_HUMAN) -  Carbonic anhydrase 4
Seq:
Struc:
312 a.a.
249 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     cell surface   19 terms 
  Biological process     small molecule metabolic process   6 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.bmc.2010.03.014 Bioorg Med Chem 18:3307-3319 (2010)
PubMed id: 20363633  
 
 
Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation.
W.Vernier, W.Chong, D.Rewolinski, S.Greasley, T.Pauly, M.Shaw, D.Dinh, R.A.Ferre, J.W.Meador, S.Nukui, M.Ornelas, R.L.Paz, E.Reyner.
 
  ABSTRACT  
 
A novel series of potent thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV was discovered using structure-based drug design. Synthesis, structure-activity relationship, and optimization of physicochemical properties are described. Low nanomolar potency was achieved, and selected compounds with improved thermodynamic solubility showed promising in vitro inhibition of carbonic anhydrase activity in rabbit iris ciliary body homogenate.