1FLG
CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA
Replaces: 1EEEFunctional 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 | 0020037 | molecular_function | heme binding |
| 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 |
| A | 0070968 | molecular_function | pyrroloquinoline quinone binding |
| 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 | 0020037 | molecular_function | heme binding |
| 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 |
| B | 0070968 | molecular_function | pyrroloquinoline quinone binding |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 116 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10736230","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10736230","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FLG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
