GL1X · GenesisL1 explorer

MolNFT v1 · #181418 · protein

Cryo-EM structure of rsv pref bound by fabs 32.4K and 01.4B

7LUC · Fusion glycoprotein F0: “Cryo-EM structure of rsv pref bound by fabs 32.4K and 01.4B”. Electron microscopy, 20 pockets (best druggability 0.85). MolNFT v1 #181418 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7LUC
Type
protein
Length
2,754 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fusion glycoprotein F0; 01.4B Fab heavy chain; 01.4B Fab light chain; 32.4K Fab heavy…
UniProt
C3UPB8
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 5 distinct chains · 17% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CFusion glycoprotein F0protein44932% helix, 30% strandC3UPB8
D, F, H01.4B Fab heavy chainprotein1217% helix, 49% strand—
E, G, I01.4B Fab light chainprotein1120% helix, 43% strand—
J, L, N32.4K Fab heavy chainprotein1295% helix, 48% strand—
K, M, O32.4K Fab light chainprotein1070% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19800.850.8693empty
210330.840.85120empty
39270.770.8074empty
48650.760.8067empty
510820.760.7877empty

Interfaces

30 interfaces between chains.

  • A–B · 2072 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 2059 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 2008 Ų buried · 14 hydrogen bonds · protein-protein
  • N–O · 967 Ų buried · 4 hydrogen bonds · protein-protein
  • L–M · 957 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 33 disulfide (disulfide).

Compared structures

  • 7LUC · Cryo-EM structure of RSV preF bound by Fabs 32.4K and 01.4B · the same entry in another collection · chain A against A, TM-score 1.00

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