› 1nmq

X-ray diffraction
2.4Å resolution

Extendend Tethering: In Situ Assembly of Inhibitors

Released:
DOI: 10.2210/pdb1nmq/pdb
PDB entry 1nmq coloured by chain, front view.
PDB entry 1nmq coloured by chain, side view.
PDB entry 1nmq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In situ assembly of enzyme inhibitors using extended tethering.
Erlanson DA, Lam JW, Wiesmann C, Luong TN, Simmons RL, DeLano WL, Choong IC, Burdett MT, Flanagan WM, Lee D, Gordon EM, O'Brien T
Nat Biotechnol 21 308-14 (2003)
PMID: 12563278

Function and Biology Details

Reaction catalysed: 
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-3 subunit p17 Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 28.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand 160 2 x 160
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 68.858Å b: 89.043Å c: 96.531Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.241 0.299
Expression system: Escherichia coli

Quick links

Citations

34 review citations

Small-molecule inhibitors of protein-protein interactions: progressing towards the dream.
Arkin et al. (2004)
33 more

5 mentions without citation

The protein structures that shape caspase activity, specificity, activation and inhibition.
Fuentes-Prior et al. (2004)
4 more