1q2l

X-ray diffraction
2.2Å resolution

Crystal Structure of pitrilysin

Released:
Entry authors: Maskos K, Jozic D, Fernandez-Catalan C

Function and Biology Details

Reaction catalysed:
Preferential cleavage of -Tyr(16)-|-Leu- and -Phe(25)-|-Tyr-bonds of oxidized insulin B chain. Also acts on other substrates of less than 7 kDa such as insulin and glucagon.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3 Chain: A
Molecule details ›
Chain: A
Length: 939 amino acids
Theoretical weight: 105.23 KDa
Source organism: Escherichia coli str. K-12 substr. W3110
Expression system: Escherichia coli
UniProt:
  • Canonical: P05458 (Residues: 24-962; Coverage: 100%)
Gene names: JW2789, b2821, ptr, ptrA
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 115.2Å b: 115.2Å c: 178.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.25
Expression system: Escherichia coli