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HIV-1 protease wt (NL4-3) in complex with a darunavir derivative

Analyse HIV-1 protease wt (NL4-3) in complex with a darunavir derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LE0
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: Q8ULI9
Ligands: XUY, SO4
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Protease	protein	99	7% helix, 58% strand	Q8ULI9

Ligands and binding sites

XUY · (3r,3as,6ar)-hexahydrofuro[2,3-b]furan-3-yl [(2S,3R)-4-{[(1,3-benzothiazol-6-yl)sulfonyl](2-methylpropyl) amino}-3-hydroxy-1-phenylbutan-2-yl]carbamate · ligand · chains B, A
SO4 · Sulfate ion · ion · 5 copies · chains B, A

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	364	0.73	0.84	34	XUY

Interfaces

1 interface between chains.

B–A · 1861 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

7LE0 · HIV-1 Protease WT (NL4-3) in Complex with a Darunavir Derivative · the same entry in another collection · chain B against B, 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 Q8ULI9
Elsewhere: RCSB PDB 7LE0 · PDBe 7LE0 · UniProt Q8ULI9

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