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 401 |
| Chain | Residue |
| A | ASP169 |
| A | HIS252 |
| A | HIS269 |
| A | TRS2922 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | TRS2922 |
| A | HOH2932 |
| A | ASP119 |
| A | ASP169 |
| A | THR173 |
| A | SER239 |
| A | HIS252 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS A 2922 |
| Chain | Residue |
| A | ASP119 |
| A | ASP169 |
| A | PHE243 |
| A | HIS252 |
| A | HIS269 |
| A | ZN401 |
| A | CL501 |
| A | HOH3121 |
Functional Information from PROSITE/UniProt
| site_id | PS00060 |
| Number of Residues | 21 |
| Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. SgLGfeSGgLAAahaIhNGlT |
| Chain | Residue | Details |
| A | SER239-THR259 | |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA |
| Chain | Residue | Details |
| A | PHE243-ALA250 | |
| site_id | PS00913 |
| Number of Residues | 29 |
| Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. VLvDteivakaParflVaGmgDALatwfE |
| Chain | Residue | Details |
| A | VAL148-GLU176 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P32816","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12193646","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KQ3","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12193646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KQ3","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | ASN256 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS252 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 312 |
| Chain | Residue | Details |
| A | ASP169 | metal ligand |
| A | HIS252 | metal ligand |
| A | HIS255 | hydrogen bond acceptor, increase basicity |
| A | HIS269 | metal ligand |
