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1TA9

Crystal structure of glycerol dehydrogenase from Schizosaccharomyces pombe

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0006071biological_processglycerol metabolic process
A0006091biological_processgeneration of precursor metabolites and energy
A0008270molecular_functionzinc ion binding
A0008888molecular_functionglycerol dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0019563biological_processglycerol catabolic process
A0019564biological_processaerobic glycerol catabolic process
A0046872molecular_functionmetal ion binding
A0061613biological_processglycolytic process from glycerol
B0005739cellular_componentmitochondrion
B0006071biological_processglycerol metabolic process
B0006091biological_processgeneration of precursor metabolites and energy
B0008270molecular_functionzinc ion binding
B0008888molecular_functionglycerol dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0019563biological_processglycerol catabolic process
B0019564biological_processaerobic glycerol catabolic process
B0046872molecular_functionmetal ion binding
B0061613biological_processglycolytic process from glycerol
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1501
ChainResidue
BASP232
BHIS315
BHIS333
BGOL1402

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1502
ChainResidue
AASP232
AHIS315
AHIS333
AGOL1401

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE K A 1503
ChainResidue
AASP232
ASER235
ATHR236
ASER302
AHIS315
AGOL1401
AHOH1540
AASP182

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 1504
ChainResidue
BASP182
BASP232
BSER235
BTHR236
BHIS315
BGOL1402
BHOH1526

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ALA A 1504
ChainResidue
AALA130
AVAL190
AILE191
ATYR192
AALA1505
AHOH1623

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ALA A 1505
ChainResidue
AALA130
AALA1504
AHOH1740

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1401
ChainResidue
AASP182
AASP232
AHIS315
AHIS333
AZN1502
AK1503
AHOH1814
AHOH1871

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1402
ChainResidue
BASP182
BASP232
BHIS315
BHIS333
BZN1501
BK1504
BHOH1749

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 1403
ChainResidue
ALYS162
AALA165
ALEU170
ASER172
ASER187
ATYR204
ALEU206
AASN207
APRO208
AHOH1530
AHOH1611
AHOH1881

Functional Information from PROSITE/UniProt
site_idPS00913
Number of Residues29
DetailsADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. IFiDtdvivraPvrflIsGigDALstwvE
ChainResidueDetails
AILE211-GLU239

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of glycerol dehydrogenase from Schizosaccharomyces pombe.","authors":["Mulichak A.M."]}}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AASN319

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
BASN319

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AHIS315

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
BHIS315

239492

PDB entries from 2025-07-30

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