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Cryo-EM structure of 2:2 C-MET/NK1 complex

Analyse Cryo-EM structure of 2:2 C-MET/NK1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MOB
Type
protein
Length
1,322 residues
Chains
4
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
Pockets
20 · best druggability 0.68

Structure

electron microscopy · 2 distinct chains · 7% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHepatocyte growth factorprotein1727% helix, 26% strandP14210
C, DHepatocyte growth factor receptor (EC 2.7.10.1)protein4897% helix, 40% strandP08581

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16200.680.7756empty
26130.670.7752empty
3500.650.9517empty
43650.630.7864empty
52530.610.8032empty

Interfaces

3 interfaces between chains.

  • A–B · 1054 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 951 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 945 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 28 disulfide (disulfide).

Compared structures

  • 7MOB · Cryo-EM structure of 2:2 c-MET/NK1 complex · the same entry in another collection · chain A against A, TM-score 1.00

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