7TX2
Crystal structure of human phenylethanolamine N-methyltransferase (PNMT) in complex with (2S)-2-amino-4-(((5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(4-(7,8-dichloro-1,2,3,4-tetrahydroisoquinolin-4-yl)butyl)amino)butanoic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004603 | molecular_function | phenylethanolamine N-methyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0042418 | biological_process | epinephrine biosynthetic process |
| A | 0042423 | biological_process | catecholamine biosynthetic process |
| B | 0004603 | molecular_function | phenylethanolamine N-methyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0042418 | biological_process | epinephrine biosynthetic process |
| B | 0042423 | biological_process | catecholamine biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS01100 |
| Number of Residues | 17 |
| Details | NNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTVYQLLSAC |
| Chain | Residue | Details |
| A | LEU75-CYS91 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16363801, ECO:0000269|PubMed:17845018, ECO:0007744|PDB:2AN4, ECO:0007744|PDB:2G70, ECO:0007744|PDB:2G72 |
| Chain | Residue | Details |
| A | TYR35 | |
| B | ASP101 | |
| B | ASN106 | |
| B | ALA181 | |
| A | TYR40 | |
| A | TYR85 | |
| A | ASP101 | |
| A | ASN106 | |
| A | ALA181 | |
| B | TYR35 | |
| B | TYR40 | |
| B | TYR85 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17845018, ECO:0007744|PDB:2G70, ECO:0007744|PDB:2G72 |
| Chain | Residue | Details |
| A | GLY79 | |
| A | ASP158 | |
| B | GLY79 | |
| B | ASP158 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16363801, ECO:0007744|PDB:2AN4 |
| Chain | Residue | Details |
| A | GLU219 | |
| A | ASP267 | |
| B | GLU219 | |
| B | ASP267 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER7 | |
| B | SER7 |
