PDBe 1nlu

X-ray diffraction
1.3Å resolution

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO(2))-Arg-Leu. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pseudomonalisin Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 38.25 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P42790 (Residues: 216-585; Coverage: 63%)
Gene name: pcp
Structure domains: Rossmann fold
PSEUDO-IODOTYROSTATIN Chains: B, C
Molecule details ›
Chains: B, C
Length: 3 amino acids
Theoretical weight: 522 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P62
Unit cell:
a: 97.84Å b: 97.84Å c: 82.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.164 0.195
Expression systems:
  • Escherichia coli
  • Not provided