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1X0X

Co-Structure of Homo Sapiens Glycerol-3-Phosphate Dehydrogenase 1 complex with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0004368molecular_functionglycerol-3-phosphate dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0006116biological_processNADH oxidation
A0006127biological_processglycerophosphate shuttle
A0006734biological_processNADH metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042803molecular_functionprotein homodimerization activity
A0045821biological_processpositive regulation of glycolytic process
A0046168biological_processglycerol-3-phosphate catabolic process
A0046486biological_processglycerolipid metabolic process
A0051287molecular_functionNAD binding
A0070062cellular_componentextracellular exosome
A0071320biological_processcellular response to cAMP
A0071356biological_processcellular response to tumor necrosis factor
A0141152molecular_functionglycerol-3-phosphate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ALYS20
AHIS67
ALYS68

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
AHOH2010
AHOH2022
AHOH2039
AHOH2049
AHOH2076
AHOH2134
ALYS204
AASN205
ATHR264
AGLY268
AARG269
AASN270

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
ALYS240
AVAL247
ASER248
ASER249
AHOH2175
AHOH2179

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AARG271
ALYS272
AHOH2017

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
AASN13
AGLN295
AHOH2065
AHOH2096
AHOH2211

site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD A 2001
ChainResidue
ASER11
AGLY12
AASN13
ATRP14
AGLY15
APHE41
ATYR63
AVAL93
APRO94
APHE97
AILE119
ALYS120
AASN151
AALA153
AARG269
AGLY294
AGLN295
ALYS296
AGLN298
AHOH2007
AHOH2011
AHOH2012
AHOH2022
AHOH2023
AHOH2039
AHOH2044
AHOH2087
AHOH2134
AHOH2135

Functional Information from PROSITE/UniProt
site_idPS00957
Number of Residues22
DetailsNAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. GALKNVVAvGaGFcdGLgFGdN
ChainResidueDetails
AGLY201-ASN222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ALYS204

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16460752
ChainResidueDetails
AGLY10
APHE41
APHE97
AALA153
AARG269
ALYS296
AGLN298

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS120

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER154

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P13707
ChainResidueDetails
ALYS289

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O35077
ChainResidueDetails
ATYR326

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
ALYS204
ATHR264

222624

PDB entries from 2024-07-17

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