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PDBsum entry 1xeg

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protein ligands metals links
Lyase PDB id
1xeg
Jmol
Contents
Protein chain
258 a.a. *
Ligands
ACT
Metals
_ZN
Waters ×243
* Residue conservation analysis
PDB id:
1xeg
Name: Lyase
Title: Crystal structure of human carbonic anhydrase ii complexed w acetate ion
Structure: Carbonic anhydrase ii. Chain: a. Synonym: carbonate dehydratase ii, ca-ii, carbonic anhydras engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.81Å     R-factor:   0.180     R-free:   0.210
Authors: P.A.Mazumdar,D.Kumaran,A.K.Das,S.Swaminathan
Key ref: P.A.Mazumdar et al. (2008). A novel acetate-bound complex of human carbonic anhydrase II. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 163-166. PubMed id: 18323598
Date:
10-Sep-04     Release date:   27-Sep-05    
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)
matches with 75.00% similarity
+ 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    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:163-166 (2008)
PubMed id: 18323598  
 
 
A novel acetate-bound complex of human carbonic anhydrase II.
P.A.Mazumdar, D.Kumaran, S.Swaminathan, A.K.Das.
 
  ABSTRACT  
 
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate-bound complex belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 71.8, c = 74.0 A. The structure was solved by the molecular-replacement method and refined to an R value of 0.18 and an R(free) of 0.21. The acetate molecule replaced the zinc-bound water molecule in the structure, differing from previous reports regarding the site of acetate binding. This mode of binding disrupts the hydrogen-bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.