GL1X · GenesisL1 explorer

MolNFT v1 · #28709 · protein

Anti-HCV Fab 19D9D6 complexed with protein L (ppl) mutant A66W

1YMH · Fab 16D9D6, light chain: “Anti-HCV Fab 19D9D6 complexed with protein L (ppl) mutant A66W”. X-ray diffraction, 16 pockets (best druggability 0.65). MolNFT v1 #28709 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
1YMH
Type
protein
Length
1,006 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab 16D9D6, light chain; Fab 16D9D6, heavy chain; Protein L
UniProt
Q51918
Pockets
16 · best druggability 0.65

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CFab 16D9D6, light chainprotein2205% helix, 44% strand—
B, DFab 16D9D6, heavy chainprotein21810% helix, 49% strand—
E, FProtein Lprotein6529% helix, 40% strandQ51918

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17520.650.7486empty
22910.620.8055empty
34910.600.7473empty
42150.580.8035empty
51340.550.8224empty

Interfaces

9 interfaces between chains.

  • A–B · 1986 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 1896 Ų buried · 15 hydrogen bonds · protein-protein
  • A–E · 735 Ų buried · 12 hydrogen bonds · protein-protein
  • C–F · 626 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 598 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 1YMH · anti-HCV Fab 19D9D6 complexed with protein L (PpL) mutant A66W · the same entry in another collection · chain A against A, TM-score 1.00

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