Research workbench

HIV-1 RT/HBY 097

Analyse HIV-1 RT/HBY 097 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BQM
Type: protein
Length: 986 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Reverse transcriptase
EC: 2.7.7.49
UniProt: P03366
Ligands: HBY
Pockets: 13 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Reverse transcriptase (EC 2.7.7.49)	protein	556	29% helix, 16% strand	P03366
B	Reverse transcriptase (EC 2.7.7.49)	protein	430	29% helix, 14% strand	P03366

Ligands and binding sites

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

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

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1030	0.80	0.81	110	HBY
2	621	0.79	0.84	66	empty
3	755	0.79	0.82	71	empty
4	292	0.65	0.81	43	empty
5	249	0.60	0.79	34	empty

Interfaces

1 interface between chains.

A–B · 2466 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

1BQM · HIV-1 RT/HBY 097 · 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 1BQM · PDBe 1BQM · UniProt P03366

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