1orf

X-ray diffraction
2.4Å resolution

The Oligomeric Structure of Human Granzyme A Reveals the Molecular Determinants of Substrate Specificity

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-, -Lys-|- >> -Phe-|- in small molecule substrates.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146263 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Granzyme A Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 25.87 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P12544 (Residues: 29-262; Coverage: 99%)
Gene names: CTLA3, GZMA, HFSP
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2221
Unit cell:
a: 115.034Å b: 145.022Å c: 39.555Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.232
Expression system: Komagataella pastoris