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Crystal structure of HIV-1 protease NL4-3 V82I mutant in complex with darunavir

Analyse Crystal structure of HIV-1 protease NL4-3 V82I mutant in complex with darunavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DH3
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: Q6B6C5
Ligands: 017, SO4
Pockets: 1 · best druggability 0.72

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Protease	protein	99	7% helix, 55% strand	Q6B6C5

Ligands and binding sites

017 · (3r,3as,6ar)-hexahydrofuro[2,3-b]furan-3-yl(1s,2r)-3-[[(4-aminophenyl)sulfonyl](isobutyl)amino]-1-benzyl-2-hydroxypropylcarbamate · ligand · chains B, A
SO4 · Sulfate ion · ion · 2 copies · chains 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	360	0.72	0.84	35	017

Interfaces

1 interface between chains.

B–A · 1849 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

6DH3 · Crystal structure of HIV-1 Protease NL4-3 V82I Mutant in complex with darunavir · 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 Q6B6C5
Elsewhere: RCSB PDB 6DH3 · PDBe 6DH3 · UniProt Q6B6C5

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