MolNFT v1 · #2241 · protein

Tyr 188 leu HIV-1 RT/HBY 097

1BQN · Reverse transcriptase: “Tyr 188 leu HIV-1 RT/HBY 097”. X-ray diffraction, 1 ligand (HBY), 13 pockets (best druggability 0.83). MolNFT v1 #2241 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1BQN
Type: protein
Length: 988 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 0.83

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Reverse transcriptase (EC 2.7.7.49)	protein	558	28% helix, 20% strand	P03366
B	Reverse transcriptase (EC 2.7.7.49)	protein	430	31% helix, 12% 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

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	905	0.83	0.85	82	HBY
2	589	0.78	0.84	51	empty
3	779	0.78	0.82	79	empty
4	526	0.73	0.82	62	empty
5	312	0.63	0.79	35	empty

Interfaces

1 interface between chains.

A–B · 2378 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1BQN · Tyr 188 leu 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 1BQN · PDBe 1BQN · UniProt P03366

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