2ea3

X-ray diffraction
1.78Å resolution

Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin

Released:
Source organism: Cellulomonas bogoriensis
Primary publication:
Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 266-9 (2007)
PMID: 17401191

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
Macromolecule:
Preprocellulomonadin Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 18.79 KDa
Source organism: Cellulomonas bogoriensis
UniProt:
  • Canonical: A2RQE2 (Residues: 199-387; Coverage: 41%)
Gene name: cbp
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 36.19Å b: 52.49Å c: 76.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.166 0.195