1MDA
CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0042597 | cellular_component | periplasmic space |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0042597 | cellular_component | periplasmic space |
| H | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| H | 0042597 | cellular_component | periplasmic space |
| J | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| J | 0042597 | cellular_component | periplasmic space |
| L | 0009308 | biological_process | amine metabolic process |
| L | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| L | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| L | 0042597 | cellular_component | periplasmic space |
| L | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| M | 0009308 | biological_process | amine metabolic process |
| M | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| M | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| M | 0042597 | cellular_component | periplasmic space |
| M | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 0 |
| Chain | Residue |
| A | HIS53 |
| A | CYS92 |
| A | HIS95 |
| A | MET98 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 0 |
| Chain | Residue |
| B | HIS53 |
| B | CYS92 |
| B | HIS95 |
| B | MET98 |
| site_id | CUE |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | CU0 |
| A | HIS53 |
| A | CYS92 |
| A | HIS95 |
| A | MET98 |
| site_id | CUF |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| B | CU0 |
| B | HIS53 |
| B | CYS92 |
| B | HIS95 |
| B | MET98 |
| site_id | TQB |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| L | TRQ57 |
| L | TRP107 |
| site_id | TQD |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| M | TRQ57 |
| M | TRP107 |
Functional Information from PROSITE/UniProt
| site_id | PS00196 |
| Number of Residues | 14 |
| Details | COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M |
| Chain | Residue | Details |
| A | ALA85-MET98 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
