3KQP
Crystal Structure of hPNMT in Complex AdoHcy and 6-Aminoquinoline
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 2001 |
| Chain | Residue |
| A | TYR27 |
| A | ASP101 |
| A | PHE102 |
| A | LEU103 |
| A | ASN106 |
| 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 | GLN86 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ES5 A 290 |
| Chain | Residue |
| A | TYR35 |
| A | ASN39 |
| A | ARG44 |
| A | VAL53 |
| A | LYS57 |
| A | PHE182 |
| A | GLU219 |
| A | TYR222 |
| A | ASP267 |
| A | HOH2186 |
| A | HOH2187 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH B 2002 |
| Chain | Residue |
| B | TYR27 |
| B | TYR35 |
| B | TYR40 |
| B | GLY79 |
| B | SER80 |
| B | GLY81 |
| B | THR83 |
| B | TYR85 |
| B | ASP101 |
| B | PHE102 |
| B | LEU103 |
| B | ASN106 |
| B | ASP158 |
| B | VAL159 |
| B | HIS160 |
| B | ALA181 |
| B | PHE182 |
| B | CYS183 |
| B | VAL187 |
| B | TYR222 |
| B | HOH2015 |
| B | HOH2124 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ES5 B 290 |
| Chain | Residue |
| B | TYR35 |
| B | ASN39 |
| B | ARG44 |
| B | LYS57 |
| B | PHE182 |
| B | GLU219 |
| B | TYR222 |
| B | MET258 |
| B | ASP267 |
| B | HOH2102 |
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 |
