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PDBsum entry 1caz

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protein ligands metals links
Lyase(oxo-acid) PDB id
1caz
Jmol
Contents
Protein chain
258 a.a. *
Ligands
ACY
Metals
_ZN ×2
Waters ×210
* Residue conservation analysis
PDB id:
1caz
Name: Lyase(oxo-acid)
Title: Wild-type and e106q mutant carbonic anhydrase complexed with acetate
Structure: Carbonic anhydrase ii. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
1.90Å     R-factor:   0.153    
Authors: K.Hakansson,C.Briand,V.Zaitsev,Y.Xue,A.Liljas
Key ref:
K.Håkansson et al. (1994). Wild-type and E106Q mutant carbonic anhydrase complexed with acetate. Acta Crystallogr D Biol Crystallogr, 50, 101-104. PubMed id: 15299482 DOI: 10.1107/S0907444993009667
Date:
26-Feb-93     Release date:   31-Oct-93    
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
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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 = ACY)
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   20 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
DOI no: 10.1107/S0907444993009667 Acta Crystallogr D Biol Crystallogr 50:101-104 (1994)
PubMed id: 15299482  
 
 
Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.
K.Håkansson, C.Briand, V.Zaitsev, Y.Xue, A.Liljas.
 
  ABSTRACT  
 
The molecular structures of the acetate complexes of wild-type human carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase II were solved with high completeness (89-91%) to 2.1 and 1.9 A resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees. The altered active-site hydrogen-bond network caused by the mutation results in a different binding of the inhibitor in the two complexes. In the mutant, but not in the wild-type complex, a carboxylate O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the wild-type enzyme ligand hydrogen bonding to this atom is normally only found for hydrogen-bond donors. The importance of this discrimination on catalysis by the enzyme is discussed briefly.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. The positions of partially neg- atively charged atoms of some of the carbonic anhydrase-ligand com- plexes. Included are, in addition to the native water molecules 263 and 338 (zinc and deep water), atoms from formate, bisulfite, ni- trate, cyanate, Diamox, aminoben- zolamide as complexed to native human carbonic anhydrase II, and the carboxylate O atoms of bicar- bonate as complexed to cobalt(II)- substituted carbonic anhydrase and to T200H mutant carbonic anhy- drase (l-l~msson, 1992, and refer- ences therein).
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1994, 50, 101-104) copyright 1994.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  18323598 P.A.Mazumdar, D.Kumaran, S.Swaminathan, and A.K.Das (2008).
A novel acetate-bound complex of human carbonic anhydrase II.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 163-166.
PDB code: 1xeg
15894606 L.Premkumar, H.M.Greenblatt, U.K.Bageshwar, T.Savchenko, I.Gokhman, J.L.Sussman, and A.Zamir (2005).
Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog.
  Proc Natl Acad Sci U S A, 102, 7493-7498.
PDB code: 1y7w
14660577 D.A.Whittington, J.H.Grubb, A.Waheed, G.N.Shah, W.S.Sly, and D.W.Christianson (2004).
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.
  J Biol Chem, 279, 7223-7228.
PDB codes: 1rj5 1rj6
11493685 D.A.Whittington, A.Waheed, B.Ulmasov, G.N.Shah, J.H.Grubb, W.S.Sly, and D.W.Christianson (2001).
Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells.
  Proc Natl Acad Sci U S A, 98, 9545-9550.
PDB codes: 1jcz 1jd0
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