spacer
spacer

PDBsum entry 2er6
Go to PDB code: 
protein ligands links
Hydrolase/hydrolase inhibitor PDB id
2er6

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
330 a.a. *
Ligands
PRO-THR-GLU-PUK-
ARG-GLU
Waters ×321
* Residue conservation analysis
PDB id:
2er6
Name: Hydrolase/hydrolase inhibitor
Title: The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
Structure: Endothiapepsin. Chain: e. Engineered: yes. H-256 peptide. Chain: i. Engineered: yes
Source: Cryphonectria parasitica. Organism_taxid: 5116. Synthetic: yes
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.200    
Authors: J.B.Cooper,S.I.Foundling,M.Szelke,T.L.Blundell
Key ref: J.Cooper et al. (1987). The structure of a synthetic pepsin inhibitor complexed with endothiapepsin. Eur J Biochem, 169, 215-221. PubMed id: 3119339
Date:
13-Oct-90     Release date:   15-Jan-91    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P11838  (CARP_CRYPA) -  Endothiapepsin from Cryphonectria parasitica
Seq:
Struc: 		419 a.a.
330 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.23.22  - endothiapepsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.

 

 
Eur J Biochem 169:215-221 (1987)
PubMed id: 3119339  
 
 
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
J.Cooper, S.Foundling, A.Hemmings, T.Blundell, D.M.Jones, A.Hallett, M.Szelke.
 
  ABSTRACT  
 
The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X-ray diffraction at 0.20-nm resolution and refined to an agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu (R = -CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side-chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19271776 P.Liu, M.R.Marzahn, A.H.Robbins, H.Gutiérrez-de-Terán, D.Rodríguez, S.H.McClung, S.M.Stevens, C.A.Yowell, J.B.Dame, R.McKenna, and B.M.Dunn (2009).
Recombinant plasmepsin 1 from the human malaria parasite plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis.
  Biochemistry, 48, 4086-4099.
PDB code: 2r9b
11714911 N.S.Andreeva, and L.D.Rumsh (2001).
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
  Protein Sci, 10, 2439-2450.  
  8845753 C.Abad-Zapatero, R.Goldman, S.W.Muchmore, C.Hutchins, K.Stewart, J.Navaza, C.D.Payne, and T.L.Ray (1996).
Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents.
  Protein Sci, 5, 640-652.
PDB code: 1zap
8673731 G.Houen, M.T.Madsen, K.W.Harlow, P.Lønblad, and B.Foltmann (1996).
The primary structure and enzymic properties of porcine prochymosin and chymosin.
  Int J Biochem Cell Biol, 28, 667-675.  
8541448 M.Marraud, and A.Aubry (1996).
Crystal structures of peptides and modified peptides.
  Biopolymers, 40, 45-83.  
9230466 V.Grand, A.Aubry, V.Dupont, A.Vicherat, and M.Marraud (1996).
Folded structures in protonated reduced dipeptides.
  J Pept Sci, 2, 381-391.  
7567964 C.Rao-Naik, K.Guruprasad, B.Batley, S.Rapundalo, J.Hill, T.Blundell, J.Kay, and B.M.Dunn (1995).
Exploring the binding preferences/specificity in the active site of human cathepsin E.
  Proteins, 22, 168-181.  
  7703859 D.Bailey, and J.B.Cooper (1994).
A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
  Protein Sci, 3, 2129-2143.
PDB codes: 1epl 1epm 1epn 1epr
8259000 S.S.Abdel-Meguid (1993).
Inhibitors of aspartyl proteinases.
  Med Res Rev, 13, 731-778.  
1603805 A.Sali, B.Veerapandian, J.B.Cooper, D.S.Moss, T.Hofmann, and T.L.Blundell (1992).
Domain flexibility in aspartic proteinases.
  Proteins, 12, 158-170.  
1594574 J.A.Hartsuck, G.Koelsch, and S.J.Remington (1992).
The high-resolution crystal structure of porcine pepsinogen.
  Proteins, 13, 1.
PDB code: 3psg
1603809 K.Suguna, E.A.Padlan, R.Bott, J.Boger, K.D.Parris, and D.R.Davies (1992).
Structures of complexes of rhizopuspepsin with pepstatin and other statine-containing inhibitors.
  Proteins, 13, 195-205.
PDB codes: 4apr 5apr 6apr
2184298 W.J.Greenlee (1990).
Renin inhibitors.
  Med Res Rev, 10, 173-236.  
  2676515 A.Sali, B.Veerapandian, J.B.Cooper, S.I.Foundling, D.J.Hoover, and T.L.Blundell (1989).
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
  EMBO J, 8, 2179-2188.
PDB code: 5er2
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.

 

spacer
spacer