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PDBsum entry 2eu2

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protein ligands metals links
Lyase PDB id
2eu2
Jmol
Contents
Protein chain
257 a.a. *
Ligands
5DS
Metals
_ZN
Waters ×310
* Residue conservation analysis
PDB id:
2eu2
Name: Lyase
Title: Human carbonic anhydrase ii in complex with novel inhibitors
Structure: Carbonic anhydrase 2. Chain: a. Synonym: carbonic anhydrase ii, carbonate dehydratase ii, ca-ii, carbonic anhydrasE C. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
1.15Å     R-factor:   0.136     R-free:   0.166
Authors: S.Z.Fisher,L.Govindasamy,N.Boyle,M.Agbandje-Mckenna, D.N.Silverman,G.M.Blackburn,R.Mckenna
Key ref:
S.Z.Fisher et al. (2006). X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 618-622. PubMed id: 16820676 DOI: 10.1107/S1744309106020446
Date:
28-Oct-05     Release date:   11-Jul-06    
PROCHECK
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 Headers
 References

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

 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  

 

 
DOI no: 10.1107/S1744309106020446 Acta Crystallograph Sect F Struct Biol Cryst Commun 62:618-622 (2006)
PubMed id: 16820676  
 
 
X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes.
S.Z.Fisher, L.Govindasamy, N.Boyle, M.Agbandje-McKenna, D.N.Silverman, G.M.Blackburn, R.McKenna.
 
  ABSTRACT  
 
Human carbonic anhydrases (CAs) are well studied targets for the development of inhibitors for pharmaceutical applications. The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a -CF2- or -CHNH2- spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Interactions between HCA II and inhibitors. (a) BB3, (b) TDM. Hydrogen bonds are indicated by dashed red lines (distances given in Å), side chains are as labeled and the Zn atom is shown as a black sphere. Figures were generated and rendered with BobScript and Raster3D, respectively (Esnouf, 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.]; Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
 
  The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 618-622) copyright 2006.  
  Figure was selected by the author.