› 1k2i

X-ray diffraction
1.8Å resolution

Crystal Structure of Gamma-Chymotrypsin in Complex with 7-Hydroxycoumarin

Released:
DOI: 10.2210/pdb1k2i/pdb
PDB entry 1k2i coloured by chain, front view.
PDB entry 1k2i coloured by chain, side view.
PDB entry 1k2i coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of gamma-chymotrypsin in complex with 7-hydroxycoumarin.
Ghani U, Ng KK, Choudhary MI, Ullah N, James MN
J Mol Biol 314 519-25 (2001)
PMID: 11846564

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymotrypsinogen A Chain: 1
Molecule details ›
Chain: 1
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-245; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand SN1 1 x SN1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 69.852Å b: 69.852Å c: 97.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.18 0.2

Quick links

Citations

2 citation in other articles

Biochemical mechanisms underlying the pro-apoptotic activity of 7,8-dihydroxy-4-methylcoumarin in human leukemic cells.
Riveiro et al. (2008)
1 more

4 mentions without citation

Coumarin as a structural component of substrates and probes for serine and cysteine proteases.
Breidenbach et al. (2020)
3 more