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Crystal Structure of HIV-1 Protease Multiple Mutant P51 Complexed with Darunavir

Analyse Crystal Structure of HIV-1 Protease Multiple Mutant P51 Complexed with Darunavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NPT
Type: protein
Length: 99 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.66
Source: Human immunodeficiency virus 1
Molecule: Protease
UniProt: O38896
Ligands: 017
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · resolution 1.66 · 1 distinct chain · 7% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease	protein	99	7% helix, 46% strand	O38896

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 A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	171	0.52	0.78	21	empty
2	68	0.29	0.73	15	empty

Compared structures

4NPT · Crystal structure of HIV-1 protease multiple mutant P51 complexed with darunavir · 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 O38896
Elsewhere: RCSB PDB 4NPT · PDBe 4NPT · UniProt O38896

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