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Nanobody C5 bound to spike

Analyse Nanobody C5 bound to spike in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OAN
Type
protein
Length
3,510 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein; Immunoglobulin mu heavy chain
UniProt
P0DTC2
Ligands
NAG
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 19% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSpike glycoproteinprotein104921% helix, 33% strandP0DTC2
F, G, HImmunoglobulin mu heavy chainprotein1212% helix, 50% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 66 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19880.830.8486empty
29930.820.8394empty
35460.810.8742empty
45370.800.8679empty
57800.790.8364empty

Interfaces

9 interfaces between chains.

  • B–C · 4846 Ų buried · 45 hydrogen bonds · protein-protein
  • A–C · 4844 Ų buried · 46 hydrogen bonds · protein-protein
  • A–B · 4827 Ų buried · 46 hydrogen bonds · protein-protein
  • B–G · 831 Ų buried · 9 hydrogen bonds · protein-protein
  • A–F · 830 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 51 glycan, 48 disulfide (N-glycosylation, disulfide).

Compared structures

  • 7OAN · Nanobody C5 bound to Spike · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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