1JQE
Crystal Structure Analysis of Human Histamine Methyltransferase (Ile105 Polymorphic Variant) Complexed with AdoHcy and Antimalarial Drug Quinacrine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001692 | biological_process | histamine metabolic process |
| A | 0001695 | biological_process | histamine catabolic process |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006548 | biological_process | L-histidine catabolic process |
| A | 0007585 | biological_process | respiratory gaseous exchange by respiratory system |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008170 | molecular_function | N-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0046539 | molecular_function | histamine N-methyltransferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0001692 | biological_process | histamine metabolic process |
| B | 0001695 | biological_process | histamine catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006548 | biological_process | L-histidine catabolic process |
| B | 0007585 | biological_process | respiratory gaseous exchange by respiratory system |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008170 | molecular_function | N-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046539 | molecular_function | histamine N-methyltransferase activity |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 400 |
| Chain | Residue |
| A | PHE19 |
| A | SER120 |
| A | ILE142 |
| A | GLN143 |
| A | MET144 |
| A | TYR147 |
| A | QUN500 |
| A | HOH533 |
| A | HOH719 |
| A | HOH720 |
| A | HOH721 |
| A | HIS29 |
| A | HOH722 |
| A | HOH723 |
| A | HOH724 |
| A | GLY60 |
| A | GLY62 |
| A | GLU89 |
| A | PRO90 |
| A | SER91 |
| A | GLN94 |
| A | THR119 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH B 401 |
| Chain | Residue |
| B | HIS29 |
| B | GLY60 |
| B | GLY62 |
| B | ILE66 |
| B | GLU89 |
| B | PRO90 |
| B | SER91 |
| B | GLN94 |
| B | THR119 |
| B | SER120 |
| B | ILE142 |
| B | GLN143 |
| B | MET144 |
| B | TYR147 |
| B | HOH556 |
| B | HOH557 |
| B | HOH558 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE QUN A 500 |
| Chain | Residue |
| A | TYR15 |
| A | VAL16 |
| A | TYR146 |
| A | TYR147 |
| A | TRP179 |
| A | TRP183 |
| A | ASP193 |
| A | LEU195 |
| A | CYS196 |
| A | PHE243 |
| A | GLU246 |
| A | SAH400 |
| A | HOH725 |
| A | HOH726 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 402 |
| Chain | Residue |
| B | UNX403 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 403 |
| Chain | Residue |
| B | UNX402 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 404 |
| Chain | Residue |
| B | UNX376 |
| B | UNX405 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 405 |
| Chain | Residue |
| B | UNX404 |
| B | UNX406 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 406 |
| Chain | Residue |
| B | UNX405 |
| B | UNX407 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 376 |
| Chain | Residue |
| B | UNX404 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 407 |
| Chain | Residue |
| B | UNX406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
