GL1X · GenesisL1 explorer

Research workbench

Crystal structure of capsid P domain of norovirus GI.3 VA115

Analyse Crystal structure of capsid P domain of norovirus GI.3 VA115 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7ER0
Type
protein
Length
1,208 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid P domain
Pockets
13 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 9% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid P domainprotein30310% helix, 33% strand—
BCapsid P domainprotein3009% helix, 32% strand—
CCapsid P domainprotein3039% helix, 33% strand—
DCapsid P domainprotein3029% helix, 33% strand—

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12810.790.9157empty
29870.780.80112empty
31620.720.9030empty
4670.720.9722empty
51360.710.9136empty

Interfaces

6 interfaces between chains.

  • C–D · 1796 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1780 Ų buried · 13 hydrogen bonds · protein-protein
  • A–D · 534 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 496 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 219 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 7ER0 · Crystal structure of capsid P domain of norovirus GI.3 VA115 · the same entry in another collection · chain D against D, TM-score 1.00

Analyse

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