1okx

X-ray diffraction
2.8Å resolution

Binding Structure of Elastase Inhibitor Scyptolin A

Released:
Source organisms:
Primary publication:
Binding structure of elastase inhibitor scyptolin A.
Chem. Biol. 10 997-1001 (2003)
PMID: 14583266

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsin-like elastase family member 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00772 (Residues: 27-266; Coverage: 96%)
Gene names: CELA1, ELA1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
SCYPTOLIN A Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 986 Da
Source organism: Scytonema hofmannii

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: P622
Unit cell:
a: 155.89Å b: 155.89Å c: 91.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.26