› 5qbc

X-ray diffraction
1.45Å resolution

Crystal structure of Endothiapepsin-FRG164 complex

Released:
DOI: 10.2210/pdb5qbc/pdb
PDB entry 5qbc coloured by chain, front view.
PDB entry 5qbc coloured by chain, side view.
PDB entry 5qbc coloured by chain, top view.
Source organism: Cryphonectria parasitica
Entry author: Huschmann F

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
UniProt:
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease

Ligands and Environments

3 bound ligands:
Ligand GOL 3 x GOL
Ligand ACT 1 x ACT
Ligand D74 1 x D74
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 45.267Å b: 73.203Å c: 52.916Å
α: 90° β: 109.39° γ: 90°
R-values:
R R work R free
0.14 0.139 0.168

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