Research workbench
Co-crystal structure of human nicotinamide N-methyltransferase (nnmt) with the tricyclic inhibitor (3)
Analyse Co-crystal structure of human nicotinamide N-methyltransferase (nnmt) with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BLE
- Type
- protein
- Length
- 1,036 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P40261
- Ligands
- U1W
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 266 | — | P40261 |
| B | — | protein | 264 | — | P40261 |
| C, D | — | protein | 253 | — | P40261 |
Ligands and binding sites
- U1W · 3-ethyl-1,3-diazatricyclo[6.3.1.0^{4,12}]dodeca-4,6, 8(12)-trien-2-imine · 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
- 7BLE · Co-crystal structure of Human Nicotinamide N-methyltransferase (NNMT) with the tricyclic… · the same entry in another collection · chain A against A, TM-score 1.00
- P40261 · AlphaFold monomer V2.0 prediction for nicotinamide N-methyltransferase (P40261) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P40261
- Elsewhere: RCSB PDB 7BLE · PDBe 7BLE · UniProt P40261
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