1JQD
Crystal Structure Analysis of Human Histamine Methyltransferase (Thr105 Polymorphic Variant) Complexed with AdoHcy and Histamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001692 | biological_process | histamine metabolic process |
| A | 0001695 | biological_process | histamine catabolic process |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| 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 | 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 | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005813 | cellular_component | centrosome |
| 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 | 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 | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 400 |
| Chain | Residue |
| A | GLY60 |
| A | GLN143 |
| A | MET144 |
| A | TYR147 |
| A | HOH631 |
| A | HOH646 |
| A | HOH773 |
| A | HOH774 |
| A | HOH775 |
| A | HOH776 |
| A | GLY62 |
| A | ILE66 |
| A | GLU89 |
| A | PRO90 |
| A | GLN94 |
| A | THR119 |
| A | SER120 |
| A | ILE142 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH B 401 |
| Chain | Residue |
| B | GLY60 |
| B | GLY62 |
| B | ILE66 |
| B | GLU89 |
| B | PRO90 |
| B | GLN94 |
| B | THR119 |
| B | SER120 |
| B | ILE142 |
| B | GLN143 |
| B | MET144 |
| B | TYR147 |
| B | HOH624 |
| B | HOH722 |
| B | HOH723 |
| B | HOH724 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HSM A 600 |
| Chain | Residue |
| A | PHE22 |
| A | GLU28 |
| A | GLN143 |
| A | VAL173 |
| A | ASN283 |
| A | HOH779 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HSM B 601 |
| Chain | Residue |
| B | PHE22 |
| B | GLU28 |
| B | GLN143 |
| B | TYR146 |
| B | VAL173 |
| B | TRP179 |
| B | PHE243 |
| B | ASN283 |
| B | LEU285 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU28 | |
| B | GLU89 | |
| B | GLN94 | |
| B | SER120 | |
| B | ILE142 | |
| B | ASN283 | |
| A | GLY60 | |
| A | GLU89 | |
| A | GLN94 | |
| A | SER120 | |
| A | ILE142 | |
| A | ASN283 | |
| B | GLU28 | |
| B | GLY60 |
