2H3X
Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dehydrogenase and Azurin from Alcaligenes Faecalis (Form 3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0030058 | molecular_function | amine dehydrogenase activity |
| A | 0042597 | cellular_component | periplasmic space |
| B | 0009308 | biological_process | amine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| B | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| B | 0042597 | cellular_component | periplasmic space |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0030058 | molecular_function | amine dehydrogenase activity |
| D | 0042597 | cellular_component | periplasmic space |
| E | 0009308 | biological_process | amine metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| E | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| E | 0042597 | cellular_component | periplasmic space |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 130 |
| Chain | Residue |
| C | GLY45 |
| C | HIS46 |
| C | CYS112 |
| C | HIS117 |
| C | MET121 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU F 130 |
| Chain | Residue |
| F | MET121 |
| F | GLY45 |
| F | HIS46 |
| F | CYS112 |
| F | HIS117 |
Functional Information from PROSITE/UniProt
| site_id | PS00196 |
| Number of Residues | 17 |
| Details | COPPER_BLUE Type-1 copper (blue) proteins signature. GedYaFFCsfPgHwsi.M |
| Chain | Residue | Details |
| C | GLY105-MET121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17087503 |
| Chain | Residue | Details |
| C | HIS46 | |
| C | CYS112 | |
| C | HIS117 | |
| C | MET121 | |
| F | HIS46 | |
| F | CYS112 | |
| F | HIS117 | |
| F | MET121 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560 |
| Chain | Residue | Details |
| B | ASP81 | |
| E | ASP81 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560 |
| Chain | Residue | Details |
| B | ASP37 | |
| B | ASN109 | |
| E | ASP37 | |
| E | ASN109 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| B | THR125 | |
| E | THR125 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Tryptophylquinone => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503 |
| Chain | Residue | Details |
| B | TRQ62 | |
| E | TRQ62 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503 |
| Chain | Residue | Details |
| B | TRQ62 | |
| B | TRP113 | |
| E | TRQ62 | |
| E | TRP113 |
