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Lyase(oxo-acid) PDB id
Protein chain
258 a.a. *
Waters ×217
* Residue conservation analysis
PDB id:
Name: Lyase(oxo-acid)
Title: The structure of human carbonic anhydrase ii in complex with bromide and azide
Structure: Carbonic anhydrase ii. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
1.80Å     R-factor:   0.161    
Authors: B.M.Jonsson,K.Hakansson,A.Liljas
Key ref: B.M.Jönsson et al. (1993). The structure of human carbonic anhydrase II in complex with bromide and azide. FEBS Lett, 322, 186-190. PubMed id: 8482389 DOI: 10.1016/0014-5793(93)81565-H
02-Apr-93     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
260 a.a.
258 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
= 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   22 terms 
  Biochemical function     protein binding     5 terms  


    Added reference    
DOI no: 10.1016/0014-5793(93)81565-H FEBS Lett 322:186-190 (1993)
PubMed id: 8482389  
The structure of human carbonic anhydrase II in complex with bromide and azide.
B.M.Jönsson, K.Håkansson, A.Liljas.
The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20118557 A.Sugimoto, H.Ikeda, H.Tsukamoto, K.Kihira, M.Ishioka, J.Hirose, T.Hata, H.Fujioka, and Y.Ono (2010).
Timolol activates the enzyme activities of human carbonic anhydrase I and II.
  Biol Pharm Bull, 33, 301-306.  
19637848 S.E.Hill, J.N.Bandaria, M.Fox, E.Vanderah, A.Kohen, and C.M.Cheatum (2009).
Exploring the molecular origins of protein dynamics in the active site of human carbonic anhydrase II.
  J Phys Chem B, 113, 11505-11510.  
18451496 A.Sugimoto, H.Ikeda, H.Tsukamoto, K.Kihira, C.Takeda, J.Hirose, T.Hata, E.Baba, and Y.Ono (2008).
The mechanisms by which latanoprost free acid inhibits human carbonic anhydrase I and II.
  Biol Pharm Bull, 31, 796-801.  
18220327 N.Couto, M.J.Ramos, M.T.Fernandez, P.Rodrigues, M.T.Barros, M.L.Costa, B.J.Cabral, and M.F.Duarte (2008).
Study of doubly charged alkaline earth metal and 3-azidopropionitrile complexes by electrospray ionization mass spectrometry.
  Rapid Commun Mass Spectrom, 22, 582-590.  
18335973 V.M.Krishnamurthy, G.K.Kaufman, A.R.Urbach, I.Gitlin, K.L.Gudiksen, D.B.Weibel, and G.M.Whitesides (2008).
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
  Chem Rev, 108, 946.  
17141524 N.Couto, M.F.Duarte, M.T.Fernandez, P.Rodrigues, M.T.Barros, M.L.Costa, and B.J.Cabral (2007).
Complexation of transition metals by 3-azidopropionitrile. An electrospray ionization mass spectrometry study.
  J Am Soc Mass Spectrom, 18, 453-465.  
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
9812982 J.Q.Liu, T.Kurihara, S.Ichiyama, M.Miyagi, S.Tsunasawa, H.Kawasaki, K.Soda, and N.Esaki (1998).
Reaction mechanism of fluoroacetate dehalogenase from Moraxella sp. B.
  J Biol Chem, 273, 30897-30902.  
9860966 M.Lim, P.Hamm, and R.M.Hochstrasser (1998).
Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes.
  Proc Natl Acad Sci U S A, 95, 15315-15320.  
9265618 F.Briganti, S.Mangani, P.Orioli, A.Scozzafava, G.Vernaglione, and C.T.Supuran (1997).
Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine.
  Biochemistry, 36, 10384-10392.
PDB code: 1avn
9325279 L.M.Watkins, H.J.Mahoney, J.K.McCulloch, and F.M.Raushel (1997).
Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase.
  J Biol Chem, 272, 25596-25601.  
9336012 S.Lindskog (1997).
Structure and mechanism of carbonic anhydrase.
  Pharmacol Ther, 74, 1.  
7705355 C.Kennes, F.Pries, G.H.Krooshof, E.Bokma, J.Kingma, and D.B.Janssen (1995).
Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity.
  Eur J Biochem, 228, 403-407.  
8306976 A.Liljas, K.Håkansson, B.H.Jonsson, and Y.Xue (1994).
Inhibition and catalysis of carbonic anhydrase. Recent crystallographic analyses.
  Eur J Biochem, 219, 1.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.