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SARS-cov-2 M protein dimer (long form) in complex with YN7756_1 Fab

Analyse SARS-cov-2 M protein dimer (long form) in complex with YN7756_1 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VGR
Type
protein
Length
1,272 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
YN7756_1 Fab light chain; YN7756_1 Fab heavy chain; Membrane protein
UniProt
P0DTC5
Pockets
17 · best druggability 0.79

Structure

electron microscopy · 3 distinct chains · 17% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, EYN7756_1 Fab light chainprotein2186% helix, 51% strand—
D, FYN7756_1 Fab heavy chainprotein2204% helix, 47% strand—
A, BMembrane proteinprotein19843% helix, 20% strandP0DTC5

Pockets

17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14500.790.8748empty
24630.590.7460empty
3940.570.8624empty
4990.560.8520empty
53740.560.7457empty

Interfaces

11 interfaces between chains.

  • A–B · 3074 Ų buried · 8 hydrogen bonds · protein-protein
  • E–F · 1865 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 1860 Ų buried · 17 hydrogen bonds · protein-protein
  • D–A · 549 Ų buried · 5 hydrogen bonds · protein-protein
  • F–B · 544 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7VGR · SARS-CoV-2 M protein dimer (long form) in complex with YN7756_1 Fab · the same entry in another collection · chain C against C, TM-score 1.00

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