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Molecular structure for the HIV-1 GP120 trimer in the unliganded state

Analyse Molecular structure for the HIV-1 GP120 trimer in the unliganded state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DNN
Type
protein
Length
864 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HIV-1 envelope glycoprotein GP120
UniProt
P04578
Pockets
9 · best druggability 0.73

Structure

electron microscopy · 3 distinct chains · 15% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, GHIV-1 envelope glycoprotein GP120protein3543% helix, 17% strandP04578
B, E, HHIV-1 envelope glycoprotein GP120protein17012% helix, 35% strandP04578
C, F, IHIV-1 envelope glycoprotein GP120protein8310% helix, 45% strandP04578

Pockets

9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.730.9831empty
2670.720.9830empty
3680.720.9730empty
4960.620.8822empty
5880.620.8923empty

Interfaces

9 interfaces between chains.

  • H–I · 3927 Ų buried · 71 hydrogen bonds · protein-protein
  • E–F · 3918 Ų buried · 71 hydrogen bonds · protein-protein
  • B–C · 3912 Ų buried · 71 hydrogen bonds · protein-protein
  • G–H · 1426 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 1424 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 3DNN · Molecular structure for the HIV-1 gp120 trimer in the unliganded state · the same entry in another collection · chain A against A, TM-score 1.00

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