6nry

X-ray diffraction
2.18Å resolution

Crystal structure of human caspase-4

Released:
Source organism: Homo sapiens
Entry authors: Yang J, Liu Z, Shi W, Xiao TS

Function and Biology Details

Reaction catalysed:
Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-4 subunit p20 Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 32.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49662 (Residues: 92-377; Coverage: 76%)
Gene names: CASP4, ICH2
Sequence domains: Caspase domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2
Spacegroup: C2221
Unit cell:
a: 40.687Å b: 163.383Å c: 103.661Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.195 0.237
Expression system: Escherichia coli