› 1dlk

X-ray diffraction
2.14Å resolution

CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR

Released:
DOI: 10.2210/pdb1dlk/pdb
PDB entry 1dlk coloured by chain, front view.
PDB entry 1dlk coloured by chain, side view.
PDB entry 1dlk coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.
Mac Sweeney A, Birrane G, Walsh MA, O'Connell T, Malthouse JP, Higgins TM
Acta Crystallogr D Biol Crystallogr 56 280-6 (2000)
PMID: 10713514

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:
hetero hexamer
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133427 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chains: A, C
Molecule details ›
Chains: A, C
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsinogen A Chains: B, D
Molecule details ›
Chains: B, D
Length: 230 amino acids
Theoretical weight: 24.21 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-245; Coverage: 94%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
peptidic inhibitor Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 466 Da

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41212
Unit cell:
a: 121.17Å b: 121.17Å c: 116.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.245

Quick links

Citations

1 review citation

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
7 other articles

1 mention without citation

Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.
Khan et al. (2011)