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 | 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 | 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: |
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 |