PDBsum entry 4mty

Go to PDB code: 
protein ligands metals links
Lyase/lyase inhibitor PDB id
Protein chain
258 a.a.
SBW ×3
GOL ×4
Waters ×398
PDB id:
Name: Lyase/lyase inhibitor
Title: Structure at 2.1 a reolution of a helical aromatic foldamer- complex.
Structure: Carbonic anhydrase 2. Chain: a. 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: 562
1.00Å     R-factor:   0.106     R-free:   0.123
Authors: T.Ogayone,J.Buratto,B.Langlois D'Estaintot,M.Stupfel,T.Grani B.Gallois,Y.Huc
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
20-Sep-13     Release date:   11-Dec-13    
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: 10.1002/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.
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.