MolNFT v1 · #160834 · protein
Structure of nicotinamide N-methyltransferase (nnmt) in complex with inhibitor LL320
6PVS: “Structure of nicotinamide N-methyltransferase (nnmt) in complex with inhibitor LL320”. X-ray diffraction, 1 ligand (P0V). MolNFT v1 #160834 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PVS
- Type
- protein
- Length
- 1,055 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6FH49
- Ligands
- P0V
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 270 | — | Q6FH49 |
| C | — | protein | 257 | — | Q6FH49 |
| D | — | protein | 258 | — | Q6FH49 |
Ligands and binding sites
- P0V · 9-(5-{[(3R)-3-amino-3-carboxypropyl][3-(3-carbamoylphenyl)prop-2-yn-1-yl]amino}-5-deoxy-alpha-D-lyxofuranosyl)-9H-purin-6-amine · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PVS · Structure of Nicotinamide N-Methyltransferase (NNMT) in complex with inhibitor LL320 · 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 Q6FH49
- Elsewhere: RCSB PDB 6PVS · PDBe 6PVS · UniProt Q6FH49
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