› 1bxo

X-ray diffraction
0.95Å resolution

ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20) COMPLEX WITH PHOSPHONATE INHIBITOR: METHYL CYCLO[(2S)-2-[[(1R)-1-(N-(L-N-(3-METHYLBUTANOYL)VALYL-L-ASPARTYL)AMINO)-3-METHYLBUT YL] HYDROXYPHOSPHINYLOXY]-3-(3-AMINOMETHYL) PHENYLPROPANOATE

Released:
DOI: 10.2210/pdb1bxo/pdb
PDB entry 1bxo coloured by chain, front view.
PDB entry 1bxo coloured by chain, side view.
PDB entry 1bxo coloured by chain, top view.
Source organism: Penicillium janthinellum
Primary publication:
Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
Khan AR, Parrish JC, Fraser ME, Smith WW, Bartlett PA, James MN
Biochemistry 37 16839-45 (1998)
PMID: 9836576

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133571 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillopepsin-1 Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 33.47 KDa
Source organism: Penicillium janthinellum
UniProt:
  • Canonical: P00798 (Residues: 1-323; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

4 bound ligands:
Ligand MAN 2 x MAN
Ligand SO4 1 x SO4
Ligand PP7 1 x PP7
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 96.98Å b: 46.65Å c: 65.71Å
α: 90° β: 115.57° γ: 90°
R-values:
R R work R free
0.1 not available 0.125

Quick links

Citations

5 review citations

Construction and screening of vast libraries of natural product-like macrocyclic peptides using in vitro display technologies.
Bashiruddin et al. (2015)
4 more

16 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
15 more