› 7h5d

X-ray diffraction
1.91Å resolution

Crystal structure of endothiapepsin PN_cryo1 in complex with AC40075 at 100 K

Released:
DOI: 10.2210/pdb7h5d/pdb
PDB entry 7h5d coloured by chain, front view.
PDB entry 7h5d coloured by chain, side view.
PDB entry 7h5d coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryocooled crystals.
Huang CY, Aumonier S, Olieric V, Wang M
Acta Crystallogr D Struct Biol (2024)
PMID: 39052318

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

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 ACT 1 x ACT
Ligand DMS 47 x DMS
Ligand EMR 1 x EMR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 43.781Å b: 72.497Å c: 50.82Å
α: 90° β: 107.55° γ: 90°
R-values:
R R work R free
0.162 0.16 0.199

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