MolNFT v1 · #30618 · protein

Synthesis and activity of N-axyl azacyclic urea HIV-1 protease inhibitors with high potency against multiple drug resistant viral strains.

2A4F · Pol polyprotein: “Synthesis and activity of N-axyl azacyclic urea HIV-1 protease inhibitors with high potency against multiple…”. X-ray diffraction, 1 ligand (AAU), 1 pocket (best druggability 0.73). MolNFT v1 #30618 on GenesisL1…

PDB: 2A4F
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 3.4.23.16
UniProt: Q9Q2G8
Ligands: AAU
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 55% strand	Q9Q2G8

Ligands and binding sites

AAU · (5R,6R)-5-benzyl-6-hydroxy-2,4-bis(4-hydroxy-3-methoxybenzyl)-1-[3-(4-hydroxyphenyl)propanoyl]-1,2,4-triazepan-3-one · ligand · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	384	0.73	0.84	37	AAU

Interfaces

1 interface between chains.

A–B · 1841 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

2A4F · Synthesis and Activity of N-Axyl Azacyclic Urea HIV-1 Protease Inhibitors with High… · 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 Q9Q2G8
Elsewhere: RCSB PDB 2A4F · PDBe 2A4F · UniProt Q9Q2G8

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