› 5v6u

X-ray diffraction
2.8Å resolution

Crystal structure of human caspase-7 soaked with allosteric inhibitor 2-[(2-acetylphenyl)sulfanyl]benzoic acid

Released:
DOI: 10.2210/pdb5v6u/pdb
PDB entry 5v6u coloured by chain, front view.
PDB entry 5v6u coloured by chain, side view.
PDB entry 5v6u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.
Vance NR, Gakhar L, Spies MA
Angew Chem Int Ed Engl 56 14443-14447 (2017)
PMID: 28940929

Function and Biology Details

Reaction catalysed: 
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157233 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 34.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 1-303; Coverage: 100%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand 8YM 1 x 8YM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P3221
Unit cell:
a: 88.393Å b: 88.393Å c: 185.358Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.191 0.245
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Proteases: Pivot Points in Functional Proteomics.
Verhamme et al. (2019)
5 other articles

1 mention without citation

Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.
Vance et al. (2017)