MolNFT v1 · #145701 · protein

Crystal structure of HCV NS3/4A wt protease in complex with aj-52 (mk- 5172 linear analogue)

6CVW · NS3 protease: “Crystal structure of HCV NS3/4A wt protease in complex with aj-52 (mk- 5172 linear analogue)”. X-ray diffraction, 3 ligands (FH1, ZN, SO4), 2 pockets (best druggability 0.42). MolNFT v1 #145701 on GenesisL1: 3D…

PDB: 6CVW
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 protease
UniProt: A0A0B4WYC6
Ligands: FH1, ZN, SO4
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 protease	protein	199	16% helix, 44% strand	A0A0B4WYC6

Ligands and binding sites

FH1 · N-[(cyclopentyloxy)carbonyl]-3-methyl-L-valyl-(4R)-N-[(1R,2S)-2-ethenyl-1-{[(1-methylcyclopropyl) sulfonyl]carbamoyl}cyclopropyl]-4-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-L-prolinamide · ligand · chains A
ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 4 copies · 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	50	0.42	0.83	15	empty
2	58	0.30	0.74	15	empty

Compared structures

6CVW · Crystal structure of HCV NS3/4A WT protease in complex with AJ-52 (MK-5172 linear… · 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 A0A0B4WYC6
Elsewhere: RCSB PDB 6CVW · PDBe 6CVW · UniProt A0A0B4WYC6

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