spacer
spacer

PDBsum entry 3po6

Go to PDB code: 
protein ligands metals links
Lyase/lyase inhibitor PDB id
3po6
Jmol
Contents
Protein chain
258 a.a.
Ligands
DT9
RDT
GOL ×4
ACT
Metals
_ZN
Waters ×313
PDB id:
3po6
Name: Lyase/lyase inhibitor
Title: Crystal structure of human carbonic anhydrase ii with 6,7-di methyl-3,4-dihydroisoquinoline-2(1h)-sulfonamide
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:
1.47Å     R-factor:   0.145     R-free:   0.175
Authors: P.Mader,J.Brynda,R.Gitto,S.Agnello,S.Ferro,L.De Luca,D.Vullo C.T.Supuran,A.Chimirri
Key ref: P.Mader et al. (2011). Structural basis for the interaction between carbonic anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides. J Med Chem, 54, 2522-2526. PubMed id: 21395315 DOI: 10.1021/jm2000213
Date:
22-Nov-10     Release date:   06-Apr-11    
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)
Bound ligand (Het Group name = ACT)
corresponds exactly
+ 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: 10.1021/jm2000213 J Med Chem 54:2522-2526 (2011)
PubMed id: 21395315  
 
 
Structural basis for the interaction between carbonic anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides.
P.Mader, J.Brynda, R.Gitto, S.Agnello, P.Pachl, C.T.Supuran, A.Chimirri, P.Řezáčová.
 
  ABSTRACT  
 
No abstract given.