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

Analyse Crystal structure of sema domain of the met receptor in complex with Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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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