› 3hmt

X-ray diffraction
2Å resolution

Crystal structure of the N-terminal fragment (28-126) of the human hepatocyte growth factor/scatter factor, trigonal crystal form

Released:
DOI: 10.2210/pdb3hmt/pdb
PDB entry 3hmt coloured by chain, front view.
PDB entry 3hmt coloured by chain, side view.
PDB entry 3hmt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for agonism and antagonism of hepatocyte growth factor.
Tolbert WD, Daugherty-Holtrop J, Gherardi E, Vande Woude G, Xu HE
Proc Natl Acad Sci U S A 107 13264-9 (2010)
PMID: 20624990

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14210 (Residues: 28-126; Coverage: 14%)
Gene names: HGF, HPTA
Sequence domains: PAN domain
Structure domains: Hepatocyte Growth Factor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P32
Unit cell:
a: 38.85Å b: 38.85Å c: 103.69Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.193 0.243
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

3 mentions without citation

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