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Human immunodeficiency virus type 1

Analyse Human immunodeficiency virus type 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HQU
Type: protein
Length: 986 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 2.7.7.49
UniProt: P03366
Ligands: HBY
Pockets: 12 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pol polyprotein (EC 2.7.7.49)	protein	556	30% helix, 21% strand	P03366
B	Pol polyprotein (EC 2.7.7.49)	protein	430	30% helix, 17% strand	P03366

Ligands and binding sites

HBY · (S)-4-isopropoxycarbonyl-6-methoxy-3-methylthiomethyl-3,4-dihydroquinoxalin-2(1H)-thione · ligand · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1010	0.82	0.83	97	empty
2	740	0.78	0.82	76	empty
3	780	0.76	0.80	76	empty
4	383	0.72	0.83	46	HBY
5	217	0.63	0.82	39	empty

Interfaces

1 interface between chains.

A–B · 2489 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

1HQU · Human immunodeficiency virus type 1 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P03366
Elsewhere: RCSB PDB 1HQU · PDBe 1HQU · UniProt P03366

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