1N7J
The structure of Phenylethanolamine N-methyltransferase in complex with S-adenosylhomocysteine and an iodinated inhibitor
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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0042418 | biological_process | epinephrine biosynthetic process |
| B | 0042423 | biological_process | catecholamine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH A 2002 |
| Chain | Residue |
| A | TYR27 |
| A | PHE102 |
| A | LEU103 |
| A | ASN106 |
| A | ILE157 |
| A | ASP158 |
| A | VAL159 |
| A | HIS160 |
| A | ALA181 |
| A | PHE182 |
| A | CYS183 |
| A | TYR35 |
| A | VAL187 |
| A | TYR40 |
| A | GLY79 |
| A | SER80 |
| A | GLY81 |
| A | THR83 |
| A | TYR85 |
| A | ASP101 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH B 2003 |
| Chain | Residue |
| B | TYR527 |
| B | TYR535 |
| B | TYR540 |
| B | GLY579 |
| B | SER580 |
| B | GLY581 |
| B | THR583 |
| B | TYR585 |
| B | ASP601 |
| B | PHE602 |
| B | LEU603 |
| B | ASN606 |
| B | ILE657 |
| B | ASP658 |
| B | VAL659 |
| B | ALA681 |
| B | PHE682 |
| B | CYS683 |
| B | VAL687 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IDI B 3002 |
| Chain | Residue |
| B | TYR535 |
| B | ASN539 |
| B | TYR540 |
| B | PHE682 |
| B | GLU719 |
| B | TYR722 |
| B | MET758 |
| B | ASP767 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IDI A 3003 |
| Chain | Residue |
| A | TYR35 |
| A | ARG44 |
| A | PHE182 |
| A | GLU219 |
| A | TYR222 |
| A | MET258 |
| A | ASP267 |
| A | HOH1052 |
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 site: {"evidences":[{"source":"PubMed","id":"16363801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17845018","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AN4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17845018","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16363801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AN4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
