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MolNFT v1 · #151857 · protein

Crystal structure of sema domain of the met receptor in complex with Fab

6I04 · Hepatocyte growth factor receptor: “Crystal structure of sema domain of the met receptor in complex with Fab”. X-ray diffraction, 18 pockets (best druggability 0.81). MolNFT v1 #151857 on GenesisL1: 3D structure, binding sites and…

PDB
6I04
Type
protein
Length
1,723 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hepatocyte growth factor receptor; Fab heavy chain; Fab light chain
EC
2.7.10.1
UniProt
P08581
Pockets
18 · best druggability 0.81

Structure

x-ray diffraction · 5 distinct chains · 6% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHepatocyte growth factor receptor (EC 2.7.10.1)protein4425% helix, 47% strandP08581
HFab heavy chainprotein2118% helix, 53% strand—
L, DFab light chainprotein2127% helix, 52% strand—
BHepatocyte growth factor receptor (EC 2.7.10.1)protein4325% helix, 47% strandP08581
CFab heavy chainprotein2147% helix, 52% strand—

Pockets

18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18520.810.8479empty
211750.800.8187empty
36840.700.7781empty
44550.670.7971empty
57180.650.7464empty

Interfaces

8 interfaces between chains.

  • C–D · 1794 Ų buried · 14 hydrogen bonds · protein-protein
  • H–L · 1669 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1582 Ų buried · 22 hydrogen bonds · protein-protein
  • A–L · 713 Ų buried · 7 hydrogen bonds · protein-protein
  • A–H · 593 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

  • 6I04 · Crystal structure of Sema domain of the Met receptor in complex with FAB · the same entry in another collection · chain A against A, TM-score 1.00

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