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PDBsum entry 4lp6

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Lyase/lyase inhibitor PDB id
4lp6
Jmol
Contents
Protein chains
257 a.a.
Ligands
Q4I ×2
Metals
_ZN ×13
Waters ×148
PDB id:
4lp6
Name: Lyase/lyase inhibitor
Title: Crystal structure of human carbonic anhydrase ii in complex quinoline oligoamide foldamer
Structure: Carbonic anhydrase 2. Chain: a, b. Synonym: carbonate dehydratase ii, carbonic anhydrasE C, ca carbonic anhydrase ii, ca-ii. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.15Å     R-factor:   0.194     R-free:   0.253
Authors: J.Buratto,T.Granier,B.Langlois D'Estaintot,I.Huc,B.Gallois
Key ref: J.Buratto et al. (2014). Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution. Angew Chem Int Ed Engl, 53, 883-887. PubMed id: 24288253 DOI: 10.1002/anie.201309160
Date:
15-Jul-13     Release date:   23-Oct-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
257 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)
+ 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: 10.1002/anie.201309160 Angew Chem Int Ed Engl 53:883-887 (2014)
PubMed id: 24288253  
 
 
Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution.
J.Buratto, C.Colombo, M.Stupfel, S.J.Dawson, C.Dolain, B.Langlois d'Estaintot, L.Fischer, T.Granier, M.Laguerre, B.Gallois, I.Huc.
 
  ABSTRACT  
 
In the search of molecules that could recognize sizeable areas of protein surfaces, a series of ten helical aromatic oligoamide foldamers was synthesized on solid phase. The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interconverting right-handed and left-handed helices. Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase II (HCA) ensured that they would be held in close proximity to the protein surface. Foldamer-protein interactions were screened by circular dichroism (CD). One foldamer displayed intense CD bands indicating that a preferred helix handedness is induced upon interacting with the protein surface. The crystal structure of the complex between this foldamer and HCA could be resolved at 2.1 Å resolution and revealed a number of unanticipated protein-foldamer, foldamer-foldamer, and protein-protein interactions.