GL1X · GenesisL1 explorer

Research workbench

Cryo-EM structure of SH1 full particle.

Analyse Cryo-EM structure of SH1 full particle. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6QT9
Type
protein
Length
5,520 residues
Chains
30
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orf 25; Orf 24; Orf 31; VP12; VP13
UniProt
Q4KPG2, Q4KPG3, Q4KPF6
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 8 distinct chains · 10% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DOrf 25protein2263% helix, 41% strandQ4KPG2
C, E, F, G, H, I, J, K, L, MOrf 25protein2254% helix, 39% strandQ4KPG2
a, b, c, d, e, f, i, j, k, m, oOrf 24protein1734% helix, 29% strandQ4KPG3
g, l, nOrf 24protein1676% helix, 36% strandQ4KPG3
hOrf 24protein1756% helix, 31% strandQ4KPG3
YOrf 31protein13512% helix, 28% strandQ4KPF6
XVP12protein2492% helix, 0% strand—
WVP13protein8054% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11730.820.9739empty
21770.820.9641empty
31640.820.9639empty
41710.810.9640empty
511030.810.82127empty

Interfaces

59 interfaces between chains.

  • F–b · 1523 Ų buried · 20 hydrogen bonds · protein-protein
  • C–m · 1521 Ų buried · 23 hydrogen bonds · protein-protein
  • I–i · 1509 Ų buried · 18 hydrogen bonds · protein-protein
  • E–c · 1473 Ų buried · 26 hydrogen bonds · protein-protein
  • A–o · 1437 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 6QT9 · Cryo-EM structure of SH1 full particle. · the same entry in another collection · chain C against C, TM-score 1.00

Analyse

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