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Crystal structure at 1.9 ångströms resolution of human immunodeficiency virus (HIV) II protease complexed with L- 735,524, an orally bioavailable inhibitor of the HIV proteases

Analyse Crystal structure at 1.9 ångströms resolution of human immunodeficiency virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HSG
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
EC: 3.4.23.-
UniProt: P03367
Ligands: MK1
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.-)	protein	99	4% helix, 56% strand	P03367

Ligands and binding sites

MK1 · N-[2(R)-hydroxy-1(S)-indanyl]-5-[(2(S)-tertiary butylaminocarbonyl)-4(3-pyridylmethyl)piperazino]-4(S)-hydroxy-2(R)-phenylmethylpentanamide · 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	386	0.73	0.84	35	MK1

Interfaces

1 interface between chains.

A–B · 1846 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

1HSG · Crystal structure at 1.9 ångströms resolution of human immunodeficiency virus (HIV) II… · 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 P03367
Elsewhere: RCSB PDB 1HSG · PDBe 1HSG · UniProt P03367

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