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PDBsum entry 4mdm

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protein ligands metals links
Lyase/lyase inhibitor PDB id
4mdm
Jmol
Contents
Protein chain
258 a.a.
Ligands
26E
Metals
_ZN
Waters ×182
PDB id:
4mdm
Name: Lyase/lyase inhibitor
Title: Nido-carborane carbonic anhydrase inhibitor
Structure: Carbonic anhydrase 2. Chain: a. Synonym: carbonate dehydratase ii, carbonic anhydrasE C, ca carbonic anhydrase ii, ca-ii. Ec: 4.2.1.1
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
1.55Å     R-factor:   0.169     R-free:   0.201
Authors: J.Brynda,P.Rezacova,P.Cigler,B.Gruner
Key ref: J.Brynda et al. (2013). Carborane-based carbonic anhydrase inhibitors. Angew Chem Int Ed Engl, 52, 13760-13763. PubMed id: 24307504 DOI: 10.1002/anie.201307583
Date:
23-Aug-13     Release date:   01-Jan-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
258 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    
 
 
DOI no: 10.1002/anie.201307583 Angew Chem Int Ed Engl 52:13760-13763 (2013)
PubMed id: 24307504  
 
 
Carborane-based carbonic anhydrase inhibitors.
J.Brynda, P.Mader, V.Šícha, M.Fábry, K.Poncová, M.Bakardiev, B.Grüner, P.Cígler, P.Řezáčová.
 
  ABSTRACT  
 
CA inhibitors: Human carbonic anhydrases (CAs) are diagnostic and therapeutic targets. Various carborane cages are shown to act as active-site-directed inhibitors, and substitution with a sulfamide group and other substituents leads to compounds with high selectivity towards the cancer-specific isozyme IX. Crystal structures of the carboranes in the active site provide information that can be applied to the structure-based design of specific inhibitors.