› 7qm6

X-ray diffraction
1.81Å resolution

Endothiapepsin in complex with compound TL00150 in 15% DMSO at 298 K

Released:
DOI: 10.2210/pdb7qm6/pdb
PDB entry 7qm6 coloured by chain, front view.
PDB entry 7qm6 coloured by chain, side view.
PDB entry 7qm6 coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.
Huang CY, Aumonier S, Engilberge S, Eris D, Smith KML, Leonarski F, Wojdyla JA, Beale JH, Buntschu D, Pauluhn A, Sharpe ME, Metz A, Olieric V, Wang M
OpenAccess logo Acta Crystallogr D Struct Biol 78 964-974 (2022)
PMID: 35916221

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: 419 amino acids
Theoretical weight: 43.28 KDa
Source organism: Cryphonectria parasitica
UniProt:
  • Canonical: P11838 (Residues: 1-419; Coverage: 100%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease

Ligands and Environments

3 bound ligands:
Ligand U1H 2 x U1H
Ligand PG5 1 x PG5
Ligand DMS 4 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 45.981Å b: 74.092Å c: 53.454Å
α: 90° β: 109.72° γ: 90°
R-values:
R R work R free
0.154 0.152 0.185

Quick links

Citations

1 review citation

A snapshot love story: what serial crystallography has done and will do for us.
Henkel et al. (2024)
9 other articles

2 mentions without citation

Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.
Huang et al. (2022)
1 more