› 1qrp

X-ray diffraction
1.96Å resolution

Human pepsin 3A in complex with a phosphonate inhibitor IVA-VAL-VAL-LEU(P)-(O)PHE-ALA-ALA-OME

Released:
DOI: 10.2210/pdb1qrp/pdb
PDB entry 1qrp coloured by chain, front view.
PDB entry 1qrp coloured by chain, side view.
PDB entry 1qrp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
Fujinaga M, Cherney MM, Tarasova NI, Bartlett PA, Hanson JE, James MN
Acta Crystallogr D Biol Crystallogr 56 272-9 (2000)
PMID: 10713513

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pepsin A-4 Chain: E
Molecule details ›
Chain: E
Length: 326 amino acids
Theoretical weight: 34.63 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P0DJD7 (Residues: 63-388; Coverage: 87%)
Gene name: PGA4
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand HH0 1 x HH0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 71.9Å b: 151.27Å c: 40.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 not available not available

Quick links

Citations

6 citation in other articles

Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Andreeva et al. (2001)
5 more

6 mentions without citation

Mechanisms of Proteolytic Enzymes and Their Inhibition in QM/MM Studies.
Elsässer et al. (2021)
5 more