3hn4

X-ray diffraction
2.6Å resolution

Crystal structure of the NK2 fragment (28-289) of human hepatocyte growth factor/scatter factor

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for agonism and antagonism of hepatocyte growth factor.
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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-146876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor alpha chain Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 30.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14210 (Residues: 28-289; Coverage: 37%)
Gene names: HGF, HPTA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D, APS BEAMLINE 21-ID-G
Spacegroup: P6522
Unit cell:
a: 48.15Å b: 48.15Å c: 461.673Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.27 0.263 0.333
Expression system: Escherichia coli