› 1fq3

X-ray diffraction
3.1Å resolution

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -Asp-|- >> -Asn-|- > -Met-|-, -Ser-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Granzyme B Chains: A, B
Molecule details ›
Chains: A, B
Length: 227 amino acids
Theoretical weight: 25.55 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P10144 (Residues: 21-247; Coverage: 99%)
Gene names: CGL1, CSPB, CTLA1, GRB, GZMB
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 41.74Å b: 114.31Å c: 135.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 not available not available
Expression system: Spodoptera frugiperda

Quick links

Citations

12 review citations

Lymphocyte-mediated cytotoxicity.
Russell et al. (2002)
11 more

10 mentions without citation

Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states.
Hashimoto et al. (2010)
9 more