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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
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019147molecular_function(R)-aminopropanol dehydrogenase activity
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
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019147molecular_function(R)-aminopropanol dehydrogenase activity
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: BINDING => ECO:0000250|UniProtKB:P32816
ChainResidueDetails
AASP37
BGLY94
BLYS95
BTHR116
BSER119
BSER125
BLEU127
BTYR131
AGLY94
ALYS95
ATHR116
ASER119
ASER125
ALEU127
ATYR131
BASP37

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:30839292, ECO:0007744|PDB:5ZXL
ChainResidueDetails
AASP121
AASP171
AHIS254
AHIS271
BASP121
BASP171
BHIS254
BHIS271

223166

PDB entries from 2024-07-31

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