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8GOA

Crystal Structure of Glycerol Dehydrogenase in the absence 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
C0005829cellular_componentcytosol
C0006071biological_processglycerol metabolic process
C0008270molecular_functionzinc ion binding
C0008888molecular_functionglycerol dehydrogenase (NAD+) activity
C0015980biological_processenergy derivation by oxidation of organic compounds
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0019147molecular_function(R)-aminopropanol dehydrogenase activity
C0019563biological_processglycerol catabolic process
C0019588biological_processanaerobic glycerol catabolic process
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
C0051596biological_processmethylglyoxal catabolic process
D0005829cellular_componentcytosol
D0006071biological_processglycerol metabolic process
D0008270molecular_functionzinc ion binding
D0008888molecular_functionglycerol dehydrogenase (NAD+) activity
D0015980biological_processenergy derivation by oxidation of organic compounds
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0019147molecular_function(R)-aminopropanol dehydrogenase activity
D0019563biological_processglycerol catabolic process
D0019588biological_processanaerobic glycerol catabolic process
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
D0051596biological_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 Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32816","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30839292","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZXL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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