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3K96

2.1 Angstrom resolution crystal structure of glycerol-3-phosphate dehydrogenase (gpsA) from Coxiella burnetii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0006629biological_processlipid metabolic process
A0006650biological_processglycerophospholipid metabolic process
A0008654biological_processphospholipid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046167biological_processglycerol-3-phosphate biosynthetic process
A0046168biological_processglycerol-3-phosphate catabolic process
A0046474biological_processglycerophospholipid biosynthetic process
A0047952molecular_functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
A0051287molecular_functionNAD binding
A0141152molecular_functionglycerol-3-phosphate dehydrogenase (NAD+) activity
A0141153molecular_functionglycerol-3-phosphate dehydrogenase (NADP+) activity
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006072biological_processglycerol-3-phosphate metabolic process
B0006629biological_processlipid metabolic process
B0006650biological_processglycerophospholipid metabolic process
B0008654biological_processphospholipid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046167biological_processglycerol-3-phosphate biosynthetic process
B0046168biological_processglycerol-3-phosphate catabolic process
B0046474biological_processglycerophospholipid biosynthetic process
B0047952molecular_functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
B0051287molecular_functionNAD binding
B0141152molecular_functionglycerol-3-phosphate dehydrogenase (NAD+) activity
B0141153molecular_functionglycerol-3-phosphate dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME B 401
ChainResidue
BSER38
BASP42
BCYS67

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EPE B 402
ChainResidue
BGLN45
BLYS64
BTYR66
BCYS67
BASP68
BHOH481

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EPE A 403
ChainResidue
AGLN45
ATYR66
ACYS67
AASP68

Functional Information from PROSITE/UniProt
site_idPS00957
Number of Residues22
DetailsNAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. GSVKNILAiAtGIsdGLkLGsN
ChainResidueDetails
AGLY189-ASN210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00394","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00394","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
ALYS192
ATHR249

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
BLYS192
BTHR249

246704

PDB entries from 2025-12-24

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