5YJI
Co-crystal structure of Mouse Nicotinamide N-methyltransferase (NNMT) with small molecule analog of Nicotinamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006769 | biological_process | nicotinamide metabolic process |
| A | 0008112 | molecular_function | nicotinamide N-methyltransferase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0031100 | biological_process | animal organ regeneration |
| A | 0032259 | biological_process | methylation |
| A | 0045722 | biological_process | positive regulation of gluconeogenesis |
| A | 0090312 | biological_process | positive regulation of protein deacetylation |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006769 | biological_process | nicotinamide metabolic process |
| B | 0008112 | molecular_function | nicotinamide N-methyltransferase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0031100 | biological_process | animal organ regeneration |
| B | 0032259 | biological_process | methylation |
| B | 0045722 | biological_process | positive regulation of gluconeogenesis |
| B | 0090312 | biological_process | positive regulation of protein deacetylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue SAH A 301 |
| Chain | Residue |
| A | TYR20 |
| A | THR87 |
| A | ASN90 |
| A | CYS141 |
| A | ASP142 |
| A | VAL143 |
| A | THR163 |
| A | LEU164 |
| A | ALA169 |
| A | 8WO302 |
| A | HOH485 |
| A | TYR25 |
| A | HOH491 |
| A | GLY63 |
| A | SER64 |
| A | GLY65 |
| A | THR67 |
| A | TYR69 |
| A | ASP85 |
| A | TYR86 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 8WO A 302 |
| Chain | Residue |
| A | TYR20 |
| A | TYR24 |
| A | LEU164 |
| A | ALA198 |
| A | SER201 |
| A | TYR204 |
| A | SER213 |
| A | TYR242 |
| A | SER247 |
| A | SAH301 |
| A | HOH436 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue SAH B 301 |
| Chain | Residue |
| B | TYR20 |
| B | TYR25 |
| B | GLY63 |
| B | SER64 |
| B | GLY65 |
| B | THR67 |
| B | TYR69 |
| B | GLN70 |
| B | ASP85 |
| B | TYR86 |
| B | THR87 |
| B | ASN90 |
| B | ASP142 |
| B | VAL143 |
| B | THR163 |
| B | LEU164 |
| B | CYS165 |
| B | 8WO302 |
| B | HOH458 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue 8WO B 302 |
| Chain | Residue |
| B | TYR20 |
| B | TYR24 |
| B | LEU164 |
| B | ALA198 |
| B | SER201 |
| B | TYR204 |
| B | SER213 |
| B | TYR242 |
| B | SER247 |
| B | SAH301 |
| B | HOH417 |
Functional Information from PROSITE/UniProt
| site_id | PS01100 |
| Number of Residues | 17 |
| Details | NNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQLLSAC |
| Chain | Residue | Details |
| A | LEU59-CYS75 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29483571, ECO:0000269|Ref.6 |
| Chain | Residue | Details |
| A | TYR20 | |
| B | TYR20 | |
| B | TYR25 | |
| B | GLY63 | |
| B | TYR69 | |
| B | ASP85 | |
| B | THR87 | |
| B | ASN90 | |
| B | ASP142 | |
| B | THR163 | |
| A | TYR25 | |
| A | GLY63 | |
| A | TYR69 | |
| A | ASP85 | |
| A | THR87 | |
| A | ASN90 | |
| A | ASP142 | |
| A | THR163 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P40261 |
| Chain | Residue | Details |
| A | ASP197 | |
| A | SER213 | |
| B | ASP197 | |
| B | SER213 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | MOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:P40261 |
| Chain | Residue | Details |
| A | ARG18 | |
| A | ARG132 | |
| A | ARG181 | |
| B | ARG18 | |
| B | ARG132 | |
| B | ARG181 |
