MolNFT v1 · #9202 · protein

Inhibition of human immunodeficiency virus-1 protease by a C2- symmetric phosphinate synthesis and crystallographic analysis

1HOS · HIV-1 protease: “Inhibition of human immunodeficiency virus-1 protease by a C2- symmetric phosphinate synthesis and…”. X-ray diffraction, 1 ligand (PHP), 1 pocket (best druggability 0.69). MolNFT v1 #9202 on GenesisL1: 3D structure…

PDB: 1HOS
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
UniProt: P03366
Ligands: PHP
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease	protein	99	4% helix, 54% strand	P03366

Ligands and binding sites

PHP · (2-phenyl-1-carbobenzyl-oxyvalyl-amino)-ethyl-phosphinic acid · 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	399	0.69	0.81	41	PHP

Interfaces

1 interface between chains.

A–B · 1811 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

1HOS · Inhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate… · 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 1HOS · PDBe 1HOS · UniProt P03366

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