Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2PLA

Crystal structure of human glycerol-3-phosphate dehydrogenase 1-like protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0002027biological_processregulation of heart rate
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0010765biological_processpositive regulation of sodium ion transport
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0017080molecular_functionsodium channel regulator activity
A0019674biological_processNAD+ metabolic process
A0042803molecular_functionprotein homodimerization activity
A0044325molecular_functiontransmembrane transporter binding
A0046168biological_processglycerol-3-phosphate catabolic process
A0047952molecular_functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
A0051287molecular_functionNAD binding
A0060373biological_processregulation of ventricular cardiac muscle cell membrane depolarization
A0070062cellular_componentextracellular exosome
A0086005biological_processventricular cardiac muscle cell action potential
A2000010biological_processpositive regulation of protein localization to cell surface
B0002027biological_processregulation of heart rate
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0006072biological_processglycerol-3-phosphate metabolic process
B0010765biological_processpositive regulation of sodium ion transport
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0017080molecular_functionsodium channel regulator activity
B0019674biological_processNAD+ metabolic process
B0042803molecular_functionprotein homodimerization activity
B0044325molecular_functiontransmembrane transporter binding
B0046168biological_processglycerol-3-phosphate catabolic process
B0047952molecular_functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
B0051287molecular_functionNAD binding
B0060373biological_processregulation of ventricular cardiac muscle cell membrane depolarization
B0070062cellular_componentextracellular exosome
B0086005biological_processventricular cardiac muscle cell action potential
B2000010biological_processpositive regulation of protein localization to cell surface
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
ALYS206
AASN207
ATHR266
AGLY270
AARG271
AASN272
AHOH507
AHOH566

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BASN207
BTHR266
BGLY270
BARG271
BASN272
BHOH602
BHOH604
BHOH610
BHOH643
BLYS206

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
ALYS22
AHIS69
ALYS70
ALYS320

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BLYS22
BLYS70

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD A 401
ChainResidue
AGLY14
AASN15
ATRP16
AGLY17
APHE43
ATYR65
APHE99
AARG102
AILE121
ALYS122
AASN153
AALA155
AARG271
AGLY296
AGLN297
ALYS298
AHOH506
AHOH566
AHOH567
AHOH574
AHOH575
AHOH576
AHOH582
AHOH588

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 401
ChainResidue
BGLY14
BASN15
BTRP16
BGLY17
BPHE43
BTYR65
BVAL94
BPRO96
BPHE99
BLEU120
BILE121
BLYS122
BASN153
BILE154
BALA155
BARG271
BGLY296
BGLN297
BLYS298
BGLN300
BHOH604
BHOH610
BHOH619
BHOH643

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of human glycerol-3-phosphate dehydrogenase 1-like protein.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
ATHR266
ALYS206

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
BTHR266
BLYS206

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon