› 1bxq

X-ray diffraction
1.41Å resolution

ACID PROTEINASE (PENICILLOPEPSIN) COMPLEX WITH PHOSPHONATE INHIBITOR.

Released:
DOI: 10.2210/pdb1bxq/pdb
PDB entry 1bxq coloured by chain, front view.
PDB entry 1bxq coloured by chain, side view.
PDB entry 1bxq 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

5 bound ligands:
Ligand MAN 2 x MAN
Ligand SO4 2 x SO4
Ligand ACT 1 x ACT
Ligand PP8 1 x PP8
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 95.829Å b: 46.431Å c: 65.186Å
α: 90° β: 115.39° γ: 90°
R-values:
R R work R free
0.143 not available 0.182

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

3 mentions without citation

Structural and thermodynamic analysis of the GFP:GFP-nanobody complex.
Kubala et al. (2010)
2 more