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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
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
C0005829cellular_componentcytosol
C0006071biological_processglycerol metabolic process
C0008270molecular_functionzinc ion binding
C0008888molecular_functionglycerol dehydrogenase (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019147molecular_function(R)-aminopropanol dehydrogenase activity
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
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019147molecular_function(R)-aminopropanol dehydrogenase activity
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: BINDING => ECO:0000250|UniProtKB:P32816
ChainResidueDetails
AASP37
BGLY94
BLYS95
BTHR116
BSER119
BSER125
BLEU127
BTYR131
CASP37
CGLY94
CLYS95
AGLY94
CTHR116
CSER119
CSER125
CLEU127
CTYR131
DASP37
DGLY94
DLYS95
DTHR116
DSER119
ALYS95
DSER125
DLEU127
DTYR131
ATHR116
ASER119
ASER125
ALEU127
ATYR131
BASP37

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:30839292, ECO:0007744|PDB:5ZXL
ChainResidueDetails
AASP121
CASP171
CHIS254
CHIS271
DASP121
DASP171
DHIS254
DHIS271
AASP171
AHIS254
AHIS271
BASP121
BASP171
BHIS254
BHIS271
CASP121

224572

PDB entries from 2024-09-04

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