› 2ea3

X-ray diffraction
1.78Å resolution

Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin

Released:
DOI: 10.2210/pdb2ea3/pdb
PDB 2ea3 coloured by chain and viewed from the front.
PDB 2ea3 coloured by chain and viewed from the side.
PDB 2ea3 coloured by chain and viewed from the top.
Source organism: Cellulomonas bogoriensis
Primary publication:
Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis.
Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R
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
Sequence domains:

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:
Ligand SO4 3 x SO4
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

Quick links

Citations

2 mentions without citation

Protein surface representation and analysis by dimension reduction.
Yang et al. (2012)
1 more