MolNFT v1 · #4708 · protein

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

1DW6: “Structural and kinetic analysis of drug resistant mutants of HIV-1 protease”. X-ray diffraction, 1 ligand (0Q4), 1 pocket (best druggability 0.68). MolNFT v1 #4708 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1DW6
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
EC: 3.4.23.16
UniProt: P03366
Ligands: 0Q4
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, D	HIV-1 protease (EC 3.4.23.16)	protein	99	7% helix, 57% strand	P03366

Ligands and binding sites

0Q4 · N-[(2R)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide · ligand · chains C, D

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	346	0.68	0.81	35	0Q4

Interfaces

1 interface between chains.

C–D · 1859 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

1DW6 · Structural and kinetic analysis of drug resistant mutants of HIV-1 protease · the same entry in another collection · chain C against C, 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 1DW6 · PDBe 1DW6 · UniProt P03366

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