› 1bmq

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF INTERLEUKIN-1BETA CONVERTING ENZYME (ICE) WITH A PEPTIDE BASED INHIBITOR, (3S )-N-METHANESULFONYL-3-({1-[N-(2-NAPHTOYL)-L-VALYL]-L-PROLYL }AMINO)-4-OXOBUTANAMIDE

Released:
DOI: 10.2210/pdb1bmq/pdb
PDB entry 1bmq coloured by chain, front view.
PDB entry 1bmq coloured by chain, side view.
PDB entry 1bmq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors: synthesis, structure activity relationships and crystallographic study of the ICE-inhibitor complex.
Okamoto Y, Anan H, Nakai E, Morihira K, Yonetoku Y, Kurihara H, Sakashita H, Terai Y, Takeuchi M, Shibanuma T, Isomura Y
Chem Pharm Bull (Tokyo) 47 11-21 (1999)
PMID: 9987822

Function and Biology Details

Reaction catalysed: 
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-151484 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-1 subunit p20 Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 18.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29466 (Residues: 131-297; Coverage: 41%)
Gene names: CASP1, IL1BC, IL1BCE
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-1 subunit p10 Chain: B
Molecule details ›
Chain: B
Length: 88 amino acids
Theoretical weight: 10.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29466 (Residues: 317-404; Coverage: 22%)
Gene names: CASP1, IL1BC, IL1BCE
Sequence domains: Caspase domain
Structure domains: Caspase-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 64.7Å b: 64.7Å c: 161.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.317
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

14 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
13 more