Research workbench

X-ray crystal structure of wild type HIV-1 protease in complex with grl-003

Analyse X-ray crystal structure of wild type HIV-1 protease in complex with grl-003 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MCS
Type: protein
Length: 99 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: Q8ULI2
Ligands: JDV
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease	protein	99	4% helix, 48% strand	Q8ULI2

Ligands and binding sites

JDV · (3S,3aR,5R,7aS,8S)-hexahydro-4H-3,5-methanofuro[2,3-b]pyran-8-yl [(2S,3R)-4-[{[2-(cyclopropylamino)-1,3-benzothiazol-6-yl]sulfonyl}(2-methylpropyl)amino]-1-(4-fluorophenyl)-3-hydroxybutan-2-yl]carbamate · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.46	0.76	20	empty
2	72	0.29	0.73	19	empty

Compared structures

6MCS · X-ray crystal structure of wild type HIV-1 protease in complex with GRL-003 · 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 Q8ULI2
Elsewhere: RCSB PDB 6MCS · PDBe 6MCS · UniProt Q8ULI2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.