1JQ5
Bacillus Stearothermophilus Glycerol dehydrogenase complex with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006071 | biological_process | glycerol metabolic process |
| A | 0008888 | molecular_function | glycerol dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0019588 | biological_process | anaerobic glycerol catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 371 |
| Chain | Residue |
| A | ASP173 |
| A | HIS256 |
| A | HIS274 |
| A | HOH402 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 372 |
| Chain | Residue |
| A | GLU268 |
| A | GLU268 |
| A | HIS271 |
| A | HIS271 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | ILE45 |
| A | GLY95 |
| A | GLY96 |
| A | LYS97 |
| A | ASP100 |
| A | THR118 |
| A | SER121 |
| A | THR122 |
| A | ASP123 |
| A | ALA124 |
| A | SER127 |
| A | LEU129 |
| A | VAL131 |
| A | TYR133 |
| A | ALA162 |
| A | PRO163 |
| A | LEU166 |
| A | PHE247 |
| A | HIS274 |
| A | HOH405 |
| A | HOH406 |
| A | HOH408 |
| A | HOH410 |
| A | HOH411 |
| A | HOH412 |
| A | HOH413 |
| A | HOH414 |
| A | ASP39 |
Functional Information from PROSITE/UniProt
| site_id | PS00060 |
| Number of Residues | 21 |
| Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. SgLGfeSGgLAAahaIhNGfT |
| Chain | Residue | Details |
| A | SER243-THR263 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA |
| Chain | Residue | Details |
| A | PHE247-ALA254 |
| site_id | PS00913 |
| Number of Residues | 29 |
| Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. VLvDtkiianaPprllAsGiaDALatwvE |
| Chain | Residue | Details |
| A | VAL152-GLU180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11566129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JQ5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11566129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JQA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11566129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JPU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JQ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JQA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | ASN260 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS256 |
