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Met receptor in complex with inlb internalin domain and darpin A3A

Analyse Met receptor in complex with inlb internalin domain and darpin A3A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GCU
Type
protein
Length
2,232 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hepatocyte growth factor receptor; Internalin B; Darpin A3A
EC
2.7.10.1
UniProt
P08581, P25147
Pockets
20 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 16% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DHepatocyte growth factor receptor (EC 2.7.10.1)protein6756% helix, 46% strandP08581
B, EInternalin Bprotein28617% helix, 25% strandP25147
C, FDarpin A3Aprotein15557% helix, 0% strand—

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111710.740.7783empty
28380.720.7754empty
39020.710.7669empty
47800.690.7666empty
5720.610.9020empty

Interfaces

6 interfaces between chains.

  • D–E · 1716 Ų buried · 32 hydrogen bonds · protein-protein
  • A–B · 1675 Ų buried · 29 hydrogen bonds · protein-protein
  • D–F · 895 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 823 Ų buried · 9 hydrogen bonds · protein-protein
  • B–E · 634 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide, 1 isopeptide (disulfide, isopeptide).

Compared structures

  • 6GCU · MET receptor in complex with InlB internalin domain and DARPin A3A · the same entry in another collection · chain A against A, TM-score 1.00

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