2AGL
Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| A | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| A | 0042597 | cellular_component | periplasmic space |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030058 | molecular_function | aliphatic amine dehydrogenase activity |
| B | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| B | 0042597 | cellular_component | periplasmic space |
| D | 0009308 | biological_process | amine metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| D | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| D | 0042597 | cellular_component | periplasmic space |
| H | 0009308 | biological_process | amine metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| H | 0030059 | molecular_function | aralkylamine dehydrogenase (azurin) activity |
| H | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PHZ H 1 |
| Chain | Residue |
| H | ASP84 |
| H | TRQ109 |
| H | ASP128 |
| H | ASN156 |
| H | VAL158 |
| H | ASN159 |
| H | PHE169 |
| H | THR172 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PHZ D 1 |
| Chain | Residue |
| D | TRQ109 |
| D | ASP128 |
| D | ASN156 |
| D | VAL158 |
| D | ASN159 |
| D | PHE169 |
| D | THR172 |
| D | ASP84 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503 |
| Chain | Residue | Details |
| A | PHE97 | |
| A | LEU100 | |
| A | ASN124 | |
| B | PHE97 | |
| B | LEU100 | |
| B | ASN124 |
| 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 |
| D | ASP128 | |
| H | ASP128 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560 |
| Chain | Residue | Details |
| D | ASP84 | |
| D | ASN156 | |
| H | ASP84 | |
| H | ASN156 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| D | THR172 | |
| H | THR172 |
| 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 |
| D | TRQ109 | |
| H | TRQ109 |
| 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 |
| D | TRQ109 | |
| D | TRP160 | |
| H | TRQ109 | |
| H | TRP160 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 2bbk |
| Chain | Residue | Details |
| D | THR172 | |
| D | ASP84 | |
| D | PHE169 | |
| D | TRP160 | |
| D | ASP128 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 2bbk |
| Chain | Residue | Details |
| H | THR172 | |
| H | ASP84 | |
| H | PHE169 | |
| H | TRP160 | |
| H | ASP128 |
