Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8GOB

Crystal Structure of Glycerol Dehydrogenase in the presence of NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006071biological_processglycerol metabolic process
A0008270molecular_functionzinc ion binding
A0008888molecular_functionglycerol dehydrogenase (NAD+) activity
A0015980biological_processenergy derivation by oxidation of organic compounds
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0019147molecular_function(R)-aminopropanol dehydrogenase activity
A0019563biological_processglycerol catabolic process
A0019588biological_processanaerobic glycerol catabolic process
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0051596biological_processmethylglyoxal catabolic process
B0005829cellular_componentcytosol
B0006071biological_processglycerol metabolic process
B0008270molecular_functionzinc ion binding
B0008888molecular_functionglycerol dehydrogenase (NAD+) activity
B0015980biological_processenergy derivation by oxidation of organic compounds
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0019147molecular_function(R)-aminopropanol dehydrogenase activity
B0019563biological_processglycerol catabolic process
B0019588biological_processanaerobic glycerol catabolic process
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0051596biological_processmethylglyoxal catabolic process
Functional Information from PROSITE/UniProt
site_idPS00060
Number of Residues21
DetailsADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. SgVGfeSGgLAAahaVhNGlT
ChainResidueDetails
ASER241-THR261

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA
ChainResidueDetails
APHE245-ALA252

site_idPS00913
Number of Residues29
DetailsADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. VIvDtkivagaParllAaGigDALatwfE
ChainResidueDetails
AVAL150-GLU178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32816","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30839292","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZXL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon