MolNFT v1 · #9417 · protein

Structural basis of drug resistance for the V82A mutant of HIV-1 protease: backbone flexibility and subsite repacking

1HVS: “Structural basis of drug resistance for the V82A mutant of HIV-1 protease: backbone flexibility and subsite…”. X-ray diffraction, 1 ligand (A77), 1 pocket (best druggability 0.69). MolNFT v1 #9417 on GenesisL1: 3D structure, binding…

PDB: 1HVS
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
UniProt: P04587
Ligands: A77
Pockets: 1 · best druggability 0.69

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease	protein	99	4% helix, 56% strand	P04587

Ligands and binding sites

A77 · N-{1-benzyl-(2R,3S)-2,3-dihydroxy-4-[3-methyl-2-(3-methyl-3-pyridin-2-ylmethyl-ureido)-butyrylamino]-5-phenyl-pentyl}-3-methyl-2-(3-methyl-3-pyridin-2-ylmethyl-ureido)-butyramide · 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	436	0.69	0.80	40	A77

Interfaces

1 interface between chains.

A–B · 1835 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

1HVS · Structural basis of drug resistance for the V82A mutant of HIV-1 protease: backbone… · 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 P04587
Elsewhere: RCSB PDB 1HVS · PDBe 1HVS · UniProt P04587

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