GL1X · GenesisL1 explorer

Research workbench

Crystal structure of tswv glycoprotein N ectodomain (trypsin treated)

Analyse Crystal structure of tswv glycoprotein N ectodomain (trypsin treated) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YA0
Type
protein
Length
553 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycoprotein
UniProt
A0A3G1GK10
Ligands
NAG, BMA, NH4
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycoproteinprotein19010% helix, 42% strandA0A3G1GK10
BGlycoproteinprotein1897% helix, 46% strandA0A3G1GK10
CGlycoproteinprotein1747% helix, 37% strandA0A3G1GK10

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains C, A, B
  • BMA · beta-D-mannopyranose · sugar
  • NH4 · Ammonium ion · ion · chains C
  • ACT · Acetate ion · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14260.590.7558empty
21400.440.7633NH4
3950.320.7320empty
4660.320.7516empty

Interfaces

2 interfaces between chains.

  • A–B · 990 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 685 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide, 6 glycan (disulfide, N-glycosylation).

Compared structures

  • 6YA0 · Crystal structure of TSWV glycoprotein N ectodomain (Trypsin treated) · 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.