2J55
X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with 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 |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| H | 0030416 | biological_process | methylamine metabolic process |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| J | 0030416 | biological_process | methylamine metabolic process |
| J | 0042597 | cellular_component | periplasmic space |
| J | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
| L | 0009308 | biological_process | amine metabolic process |
| L | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 1106 |
| Chain | Residue |
| A | HIS53 |
| A | CYS92 |
| A | HIS95 |
| A | MET98 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 1106 |
| Chain | Residue |
| B | HIS53 |
| B | CYS92 |
| B | HIS95 |
| B | MET98 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL H 1387 |
| Chain | Residue |
| H | HIS250 |
| H | LEU262 |
| H | ALA264 |
| H | HOH2277 |
| H | PHE220 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL H 1388 |
| Chain | Residue |
| H | HIS54 |
| H | TRP282 |
| H | GLN378 |
| H | HOH2392 |
| H | HOH2402 |
| L | HOH2021 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 1389 |
| Chain | Residue |
| H | GLN14 |
| H | ALA18 |
| H | ARG70 |
| H | HOH2012 |
| H | HOH2403 |
| H | HOH2405 |
| H | HOH2406 |
| M | ASP37 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL L 1132 |
| Chain | Residue |
| H | ARG305 |
| L | CYS23 |
| L | CYS88 |
| L | LEU89 |
| L | ASN90 |
| L | HOH2048 |
| L | HOH2073 |
| L | HOH2074 |
| L | HOH2075 |
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 | 208 |
| Details | Domain: {"description":"Plastocyanin-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"1409575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 2bbk |
| Chain | Residue | Details |
| L | ASP76 | |
| L | THR122 | |
| L | ASP32 | |
| L | TYR119 | |
| L | TRP108 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 2bbk |
| Chain | Residue | Details |
| M | ASP76 | |
| M | THR122 | |
| M | ASP32 | |
| M | TYR119 | |
| M | TRP108 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 13 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 13 |
| Chain | Residue | Details |






