› 3tju

X-ray diffraction
2.7Å resolution

Crystal structure of human granzyme H with an inhibitor

Released:
DOI: 10.2210/pdb3tju/pdb
PDB entry 3tju coloured by chain, front view.
PDB entry 3tju coloured by chain, side view.
PDB entry 3tju coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the substrate specificity of human granzyme H: the functional roles of a novel RKR motif.
Wang L, Zhang K, Wu L, Liu S, Zhang H, Zhou Q, Tong L, Sun F, Fan Z
J Immunol 188 765-73 (2012)
PMID: 22156497

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149045 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Granzyme H Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20718 (Residues: 21-246; Coverage: 99%)
Gene names: CGL2, CTSGL2, GZMH
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ac-PTSY-CMK inhibitor Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 527 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P41212
Unit cell:
a: 63.239Å b: 63.239Å c: 144.782Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.229 0.288
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
2 more

1 mention without citation

Chromatographic analysis of selected phytosterols from Cyathea and their characterization by in silico docking to potential therapeutic targets.
Janakiraman et al. (2023)