2HKM
Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030058 | molecular_function | 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 | 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 | 4 |
Details | BINDING SITE FOR RESIDUE PEA H 1401 |
Chain | Residue |
H | ASP84 |
H | ASP128 |
H | ASN159 |
H | THR172 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEA D 1402 |
Chain | Residue |
D | ASP84 |
D | ASP128 |
D | ASN159 |
D | PHE169 |
D | THR172 |
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 |