X-ray diffraction
0.87Å resolution

S. erythraea trypsin acyl-enzyme

Source organism: Saccharopolyspora erythraea
Entry authors: Blankenship E, Lodowski DT

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidase S1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 23.66 KDa
Source organism: Saccharopolyspora erythraea
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q54137 (Residues: 43-272; Coverage: 95%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 41.682Å b: 47.433Å c: 53.68Å
α: 90° β: 106.2° γ: 90°
R R work R free
0.106 0.106 0.121
Expression system: Escherichia coli BL21(DE3)