GL1X · GenesisL1 explorer

Research workbench

Cryoem structure of SARS-cov-2 rbd in complex with nanobodies NB21 and NB105

Analyse Cryoem structure of SARS-cov-2 rbd in complex with nanobodies NB21 and NB105 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MDW
Type
protein
Length
435 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nonobody NB21; Spike protein S1; Nanobody NB105
UniProt
P0DTC2
Ligands
NAG
Pockets
5 · best druggability 0.69

Structure

electron microscopy · 3 distinct chains · 6% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANonobody NB21protein1170% helix, 20% strand—
RSpike protein S1protein1949% helix, 30% strandP0DTC2
BNanobody NB105protein1246% helix, 29% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains R

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.690.9520empty
22110.640.8337empty
3740.640.9223empty
41960.580.8038empty
5590.420.8217empty

Interfaces

2 interfaces between chains.

  • R–B · 710 Ų buried · 11 hydrogen bonds · protein-protein
  • A–R · 630 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 7MDW · CryoEM structure of SARS-CoV-2 RBD in complex with nanobodies Nb21 and Nb105 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.