› 1gmn

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURES OF NK1-HEPARIN COMPLEXES REVEAL THE BASIS FOR NK1 ACTIVITY AND ENABLE ENGINEERING OF POTENT AGONISTS OF THE MET RECEPTOR

Released:
DOI: 10.2210/pdb1gmn/pdb
PDB entry 1gmn coloured by chain, front view.
PDB entry 1gmn coloured by chain, side view.
PDB entry 1gmn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.
Lietha D, Chirgadze DY, Mulloy B, Blundell TL, Gherardi E
EMBO J 20 5543-55 (2001)
PMID: 11597998

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146878 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Hepatocyte growth factor alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 21.17 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P14210 (Residues: 28-210; Coverage: 26%)
Gene names: HGF, HPTA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: IDS, SGN
Carbohydrate polymer
1 bound ligand:
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P43212
Unit cell:
a: 86.56Å b: 86.56Å c: 117.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.262 0.279
Expression system: Komagataella pastoris

Quick links

Citations

19 review citations

Met, metastasis, motility and more.
Birchmeier et al. (2003)
18 more

12 mentions without citation

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