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SARS-cov-2 omicron rbd in complex with omi-25 Fab

Analyse SARS-cov-2 omicron rbd in complex with omi-25 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7ZFD
Type
protein
Length
1,241 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Omi-25 heavy chain; Spike protein S1; Omi-25 light chain
UniProt
P0DTC2
Pockets
15 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 10% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H, AOmi-25 heavy chainprotein2248% helix, 48% strand—
ESpike protein S1protein18513% helix, 28% strandP0DTC2
L, BOmi-25 light chainprotein2135% helix, 48% strand—
FSpike protein S1protein18213% helix, 31% strandP0DTC2

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16950.750.8178empty
27380.670.7567empty
31750.600.8333empty
43930.570.7548empty
52250.540.7734empty

Interfaces

9 interfaces between chains.

  • H–L · 1854 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1808 Ų buried · 12 hydrogen bonds · protein-protein
  • F–B · 517 Ų buried · 10 hydrogen bonds · protein-protein
  • E–L · 498 Ų buried · 9 hydrogen bonds · protein-protein
  • H–A · 426 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 7ZFD · SARS-CoV-2 Omicron RBD in complex with Omi-25 Fab · the same entry in another collection · chain H against H, TM-score 1.00

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