› 2er7

X-ray diffraction
1.6Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEINASES.III. THREE-DIMENSIONAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH A TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN AT 1.6 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2er7/pdb
PDB entry 2er7 coloured by chain, front view.
PDB entry 2er7 coloured by chain, side view.
PDB entry 2er7 coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
Veerapandian B, Cooper JB, Sali A, Blundell TL
J Mol Biol 216 1017-29 (1990)
PMID: 2266553

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers 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.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145954 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endothiapepsin Chain: E
Molecule details ›
Chain: E
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
Expression system: Not provided
UniProt:
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN Chain: I
Molecule details ›
Chain: I
Length: 8 amino acids
Theoretical weight: 1.1 KDa
Source organism: Cryphonectria parasitica
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43Å b: 75.7Å c: 42.9Å
α: 90° β: 97° γ: 90°
R-values:
R R work R free
0.142 0.142 not available
Expression system: Not provided

Quick links

Citations

3 review citations

The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides.
Siligardi et al. (1995)
2 more

7 mentions without citation

FLEXS: a method for fast flexible ligand superposition.
Lemmen et al. (1998)
6 more