GL1X · GenesisL1 explorer

Research workbench

Immature HIV-1 matrix structure

Analyse Immature HIV-1 matrix structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OVQ
Type
protein
Length
2,760 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
7.2
Source
Human immunodeficiency virus 1
Molecule
Gag polyprotein
UniProt
B6DRA0
Ligands
MYR
Pockets
20 · best druggability 0.64

Structure

electron microscopy · resolution 7.2 · 1 distinct chain · 67% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, P, b, E, Q, c, F, R, d, S, f, I, h, K, X, M, Y, Z, l, O, mGag polyproteinprotein11567% helix, 3% strandB6DRA0

Ligands and binding sites

  • MYR · Myristic acid · ligand · 24 copies · chains A, B, C, D, P, b, E, Q, c, F, R, d, S, f, I, h, K, X, M, Y, Z, l, O, m

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18050.640.73116empty
27920.630.73122empty
34310.550.7469empty
44520.550.7360empty
54190.540.7463empty

Interfaces

24 interfaces between chains.

  • E–O · 77 Ų buried · 0 hydrogen bonds · protein-protein
  • b–l · 76 Ų buried · 0 hydrogen bonds · protein-protein
  • P–S · 75 Ų buried · 0 hydrogen bonds · protein-protein
  • F–I · 72 Ų buried · 0 hydrogen bonds · protein-protein
  • c–f · 72 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 lipid (myristoylation).

Compared structures

  • 7OVQ · Immature HIV-1 matrix structure · 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.