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

Analyse Cryo-EM structure of rsv pref bound by fabs 32.4K and 01.4B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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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