› 3hmr

X-ray diffraction
2Å resolution

Crystal structure of the N-terminal fragment (31-127) of the mouse hepatocyte growth factor/scatter factor

Released:
DOI: 10.2210/pdb3hmr/pdb
PDB entry 3hmr coloured by chain, front view.
PDB entry 3hmr coloured by chain, side view.
PDB entry 3hmr coloured by chain, top view.
Source organism: Mus musculus
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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170591 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor alpha chain Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.68 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08048 (Residues: 31-127; Coverage: 14%)
Gene name: Hgf
Sequence domains: PAN domain
Structure domains: Hepatocyte Growth Factor

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P65
Unit cell:
a: 62.42Å b: 62.42Å c: 58.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.211 0.265
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

1 mention without citation

Structural basis for agonism and antagonism of hepatocyte growth factor.
Tolbert et al. (2010)