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Cryo-EM structure of 1:1 C-met I/HGF I complex after focused 3D refinement of holo-complex

Analyse Cryo-EM structure of 1:1 C-met I/HGF I complex after focused 3D refinement of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MO8
Type
protein
Length
1,250 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hepatocyte growth factor; Hepatocyte growth factor receptor
EC
2.7.10.1
UniProt
P14210, P08581
Ligands
SGN, IDS
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 2 distinct chains · 8% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHepatocyte growth factorprotein6379% helix, 22% strandP14210
BHepatocyte growth factor receptor (EC 2.7.10.1)protein6138% helix, 37% strandP08581

Ligands and binding sites

  • SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 3 copies · chains A
  • IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110150.780.7998empty
22420.720.8753empty
36620.710.7845empty
4590.690.9521empty
56780.670.7652empty

Interfaces

1 interface between chains.

  • A–B · 2091 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 31 disulfide (disulfide).

Compared structures

  • 7MO8 · Cryo-EM structure of 1:1 c-MET I/HGF I complex after focused 3D refinement of holo-complex · the same entry in another collection · chain A against A, TM-score 1.00

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