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Structure of sybody SR4 in complex with the SARS-cov-2 S receptor binding domain (rbd)

Analyse Structure of sybody SR4 in complex with the SARS-cov-2 S receptor binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7C8V
Type
protein
Length
313 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Synthetic nanobody SR4; Spike protein S1
UniProt
P0DTC2
Ligands
NAG
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASynthetic nanobody SR4protein1195% helix, 51% strand—
BSpike protein S1protein19419% helix, 30% strandP0DTC2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B
  • GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11420.590.8425GOL

Interfaces

1 interface between chains.

  • A–B · 797 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 7C8V · Structure of sybody SR4 in complex with the SARS-CoV-2 S Receptor Binding domain (RBD) · the same entry in another collection · chain A against A, TM-score 1.00

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