› 6m9f

X-ray diffraction
1.3Å resolution

PSEUDOMONAS SERINE-CARBOXYL PROTEINASE (SEDOLISIN) COMPLEXED WITH THE INHIBITOR Tyrostatin

Released:
DOI: 10.2210/pdb6m9f/pdb
PDB entry 6m9f coloured by chain, front view.
PDB entry 6m9f coloured by chain, side view.
PDB entry 6m9f coloured by chain, top view.
Source organisms:
Primary publication:
Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.
Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K
Biochemistry 40 15602-11 (2001)
PMID: 11747435

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154883 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pseudomonalisin Chain: A
Molecule details ›
Chain: A
Length: 368 amino acids
Theoretical weight: 38.11 KDa
Source organism: Pseudomonas sp. 101
Expression system: Escherichia coli
UniProt:
  • Canonical: P42790 (Residues: 218-585; Coverage: 63%)
Gene name: pcp
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Tyrostatin Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 528 Da
Source organism: Kitasatospora
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
1 modified residue:
Ligand TYE 1 x TYE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P62
Unit cell:
a: 98.24Å b: 98.24Å c: 83.39Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 not available 0.219
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
4 more

1 mention without citation

Protocol for iterative optimization of modified peptides bound to protein targets.
Ochoa et al. (2022)