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Cryoem structure of the truncated HIV-1 VIF/CBFBETA/A3F complex

Analyse Cryoem structure of the truncated HIV-1 VIF/CBFBETA/A3F complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6NIL
Type
protein
Length
1,800 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA dc->du-editing enzyme apobec-3F; Core-binding factor subunit beta; Virion infectivity…
EC
3.5.4.38
UniProt
Q8IUX4, Q13951, P12504, A0A346ARH7
Ligands
ZN
Pockets
20 · best druggability 0.76

Structure

electron microscopy · 3 distinct chains · 27% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, G, JDNA dc->du-editing enzyme apobec-3F (EC 3.5.4.38)protein17737% helix, 16% strandQ8IUX4
B, E, H, KCore-binding factor subunit betaprotein14022% helix, 34% strandQ13951
C, F, I, LVirion infectivity factorprotein13318% helix, 28% strandP12504, A0A346ARH7

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, D, G, J

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19830.760.7894empty
29020.750.7880empty
38090.730.7874empty
46750.730.7960empty
52780.640.8139empty

Interfaces

28 interfaces between chains.

  • E–F · 2240 Ų buried · 36 hydrogen bonds · protein-protein
  • K–L · 2240 Ų buried · 36 hydrogen bonds · protein-protein
  • B–C · 2234 Ų buried · 36 hydrogen bonds · protein-protein
  • H–I · 2234 Ų buried · 36 hydrogen bonds · protein-protein
  • D–F · 726 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 6NIL · cryoEM structure of the truncated HIV-1 Vif/CBFbeta/A3F complex · the same entry in another collection · chain L against L, TM-score 1.00

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