Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0006068 | biological_process | ethanol catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
A | 0052934 | molecular_function | alcohol dehydrogenase (cytochrome c) activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0006068 | biological_process | ethanol catabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
B | 0052934 | molecular_function | alcohol dehydrogenase (cytochrome c) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 751 |
Chain | Residue |
A | GLU179 |
A | ASN266 |
A | ASP316 |
A | PQQ701 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 761 |
Chain | Residue |
A | ASP11 |
A | THR14 |
A | ASP17 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 752 |
Chain | Residue |
B | ASP316 |
B | PQQ702 |
B | GLU179 |
B | ASN266 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 762 |
Chain | Residue |
B | ASP11 |
B | THR14 |
B | ASP17 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PQQ A 701 |
Chain | Residue |
A | GLU61 |
A | CYS105 |
A | CYS106 |
A | ARG111 |
A | THR155 |
A | SER176 |
A | GLY177 |
A | ASP178 |
A | TRP248 |
A | ASN266 |
A | ARG344 |
A | ASN413 |
A | TRP414 |
A | TRP489 |
A | GLY552 |
A | ALA553 |
A | CA751 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PQQ B 702 |
Chain | Residue |
B | GLU61 |
B | CYS105 |
B | CYS106 |
B | ARG111 |
B | THR155 |
B | SER176 |
B | GLY177 |
B | ASP178 |
B | GLU179 |
B | TRP248 |
B | ASN266 |
B | ARG344 |
B | LEU409 |
B | ASN413 |
B | TRP414 |
B | TRP489 |
B | GLY552 |
B | ALA553 |
B | CA752 |
Functional Information from PROSITE/UniProt
site_id | PS00363 |
Number of Residues | 29 |
Details | BACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. DVlqyGMgthaqrWSplkqVNadNVfkLT |
Chain | Residue | Details |
A | ASP17-THR45 | |
site_id | PS00364 |
Number of Residues | 22 |
Details | BACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WqsasFDaetNTIIVgaGnpGP |
Chain | Residue | Details |
A | TRP248-PRO269 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP316 | |
B | ASP316 | |
Chain | Residue | Details |
A | ASP11 | |
A | ASP316 | |
A | ARG344 | |
A | TRP489 | |
A | ALA553 | |
B | ASP11 | |
B | THR14 | |
B | ASP17 | |
B | GLU61 | |
B | ARG111 | |
B | THR155 | |
A | THR14 | |
B | HIS173 | |
B | GLU179 | |
B | ASN266 | |
B | ASP316 | |
B | ARG344 | |
B | TRP489 | |
B | ALA553 | |
A | ASP17 | |
A | GLU61 | |
A | ARG111 | |
A | THR155 | |
A | HIS173 | |
A | GLU179 | |
A | ASN266 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g72 |
Chain | Residue | Details |
A | ASP316 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g72 |
Chain | Residue | Details |
B | ASP316 | |