3p45

X-ray diffraction
2.53Å resolution

Crystal structure of apo-caspase-6 at physiological pH

Released:
Source organism: Homo sapiens
Entry authors: Mueller I, Lamers MBAC, Ritchie AJ, Dominguez C, Munoz I, Maillard M, Kiselyov A

Function and Biology Details

Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157271 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-6 subunit p18 Chains: A, C, E, G, I, K, M, O
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 179 amino acids
Theoretical weight: 20.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 1-179; Coverage: 61%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-6 subunit p11 Chains: B, D, F, H, J, L, N, P
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 108 amino acids
Theoretical weight: 12.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 193-293; Coverage: 35%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Caspase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 81.23Å b: 161.24Å c: 88.92Å
α: 90° β: 94.8° γ: 90°
R-values:
R R work R free
0.21 0.207 0.264
Expression system: Escherichia coli