Research workbench
Crystal structure of HCV NS3/4A D168A protease in complex with NR02-08
Analyse Crystal structure of HCV NS3/4A D168A protease in complex with NR02-08 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MMJ
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0B4WYC6
- Ligands
- ZJM, ZN, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 197 | — | A0A0B4WYC6 |
Ligands and binding sites
- ZJM · (1R,2R)-2-fluorocyclopentyl {(2r,4s,6s,12z,13as,14ar, 16AS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14A-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13A,14,14A,15,16,16A-hexadecahydrocyclopropa[e]pyrrolo[1,2-A][1, 4]diazacyclopentadecin-6-yl}carbamate · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7MMJ · Crystal structure of HCV NS3/4A D168A protease in complex with NR02-08 · 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 7MMJ · PDBe 7MMJ · UniProt A0A0B4WYC6
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