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Crystal structure of HIV-1 protease mutant I54V with antiviral drug amprenavir

Analyse Crystal structure of HIV-1 protease mutant I54V with antiviral drug amprenavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NUJ
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: P03366
Ligands: 478, IOD
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease (EC 3.4.23.16)	protein	99	7% helix, 56% strand	P03366

Ligands and binding sites

478 · {3-[(4-amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid tetrahydro-furan-3-yl ester · ligand · chains A, B
IOD · Iodide ion · ion · 19 copies · 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	339	0.73	0.85	34	478

Interfaces

1 interface between chains.

A–B · 1872 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

3NUJ · Crystal Structure of HIV-1 Protease Mutant I54V with Antiviral Drug Amprenavir · 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 P03366
Elsewhere: RCSB PDB 3NUJ · PDBe 3NUJ · UniProt P03366

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