› 1si5

X-ray diffraction
2.53Å resolution

Protease-like domain from 2-chain hepatocyte growth factor

Released:
DOI: 10.2210/pdb1si5/pdb
PDB entry 1si5 coloured by chain, front view.
PDB entry 1si5 coloured by chain, side view.
PDB entry 1si5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional basis of the serine protease-like hepatocyte growth factor beta-chain in Met binding and signaling.
Kirchhofer D, Yao X, Peek M, Eigenbrot C, Lipari MT, Billeci KL, Maun HR, Moran P, Santell L, Wiesmann C, Lazarus RA
J Biol Chem 279 39915-24 (2004)
PMID: 15218027

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor beta chain Chain: H
Molecule details ›
Chain: H
Length: 240 amino acids
Theoretical weight: 26.84 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P14210 (Residues: 495-728; Coverage: 34%)
Gene names: HGF, HPTA
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P3121
Unit cell:
a: 63.7Å b: 63.7Å c: 135.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.248 0.246 0.301
Expression system: Spodoptera frugiperda

Quick links

Citations

16 review citations

Targeting MET in cancer: rationale and progress.
Gherardi et al. (2012)
15 more

4 mentions without citation

State of the structure address on MET receptor activation by HGF.
Linossi et al. (2021)
3 more