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The crystal structures at 2.2 ångströms resolution of hydroxyethylene- based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations

Analyse The crystal structures at 2.2 ångströms resolution of hydroxyethylene- based… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HEG
Type: protein
Length: 99 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
UniProt: P03366
Ligands: PSI
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	HIV-1 protease	protein	99	4% helix, 48% strand	P03366

Ligands and binding sites

PSI · methyl N-{(4S,5S)-5-[(L-alanyl-L-alanyl)amino]-4-hydroxy-6-phenylhexanoyl}-L-valyl-L-valinate · ligand · chains E

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	148	0.44	0.75	19	empty
2	67	0.32	0.75	19	empty

Compared structures

1HEG · The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors… · the same entry in another collection · chain E against E, 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 1HEG · PDBe 1HEG · UniProt P03366

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