1op8

X-ray diffraction
2.5Å resolution

Crystal Structure of Human Granzyme A

Released:
Source organism: Homo sapiens

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 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 234 amino acids
Theoretical weight: 25.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P1
Unit cell:
a: 49.48Å b: 94.55Å c: 94.87Å
α: 117.12° β: 100.25° γ: 100.12°
R-values:
R R work R free
0.218 0.218 0.284
Expression system: Escherichia coli