› 7qmq

X-ray diffraction
1.79Å resolution

Endothiapepsin in complex with compound TL00150 at room-temperature (temperature ramping down structure 18)

Released:
DOI: 10.2210/pdb7qmq/pdb
PDB entry 7qmq coloured by chain, front view.
PDB entry 7qmq coloured by chain, side view.
PDB entry 7qmq 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 3 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 45.768Å b: 73.949Å c: 53.402Å
α: 90° β: 109.607° γ: 90°
R-values:
R R work R free
0.209 0.207 0.238

Quick links

Citations

7 citation in other articles

Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi.
Mikolajek et al. (2023)
6 more

1 mention without citation

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