› 1apw

X-ray diffraction
1.8Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION STATE MIMICS BOUND TO PENICILLOPEPSIN: DIFLUOROSTATINE-AND DIFLUOROSTATONE-CONTAINING PEPTIDES

Released:
DOI: 10.2210/pdb1apw/pdb
PDB entry 1apw coloured by chain, front view.
PDB entry 1apw coloured by chain, side view.
PDB entry 1apw coloured by chain, top view.
Source organism: Penicillium janthinellum
Primary publication:
Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
James MN, Sielecki AR, Hayakawa K, Gelb MH
Biochemistry 31 3872-86 (1992)
PMID: 1567842

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133575 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Penicillopepsin-1 Chain: E
Molecule details ›
Chain: E
Length: 323 amino acids
Theoretical weight: 33.47 KDa
Source organism: Penicillium janthinellum
Expression system: Not provided
UniProt:
  • Canonical: P00798 (Residues: 1-323; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
INHIBITOR ISOVALERYL (IVA)-VAL-VAL-DIFLUOROSTATINE-N-METHYLAMINE Chain: I
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 507 Da
Source organism: Penicillium janthinellum
Expression system: Not provided

Ligands and Environments

4 bound ligands:
Ligand MAN 1 x MAN
Ligand HSY 1 x HSY
Ligand SO4 1 x SO4
Ligand DMF 1 x DMF
1 modified residue:
Ligand DFI 1 x DFI

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 97.64Å b: 46.58Å c: 66.44Å
α: 90° β: 116.12° γ: 90°
R-values:
R R work R free
0.131 not available not available
Expression system: Not provided

Quick links

Citations

7 review citations

Molecular and biotechnological aspects of microbial proteases.
Rao et al. (1998)
6 more

9 mentions without citation

Pepsin-like aspartic proteases (PAPs) as model systems for combining biomolecular simulation with biophysical experiments.
Bhakat S. (2021)
8 more