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2R4J

Crystal structure of Escherichia coli SeMet substituted Glycerol-3-phosphate Dehydrogenase in complex with DHAP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004368molecular_functionglycerol-3-phosphate dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006071biological_processglycerol metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0006796biological_processphosphate-containing compound metabolic process
A0009055molecular_functionelectron transfer activity
A0009060biological_processaerobic respiration
A0009061biological_processanaerobic respiration
A0009331cellular_componentglycerol-3-phosphate dehydrogenase (FAD) complex
A0016491molecular_functionoxidoreductase activity
A0019563biological_processglycerol catabolic process
A0019637biological_processorganophosphate metabolic process
A0042803molecular_functionprotein homodimerization activity
A0046168biological_processglycerol-3-phosphate catabolic process
A0071949molecular_functionFAD binding
B0004368molecular_functionglycerol-3-phosphate dehydrogenase (quinone) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006071biological_processglycerol metabolic process
B0006072biological_processglycerol-3-phosphate metabolic process
B0006796biological_processphosphate-containing compound metabolic process
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0009061biological_processanaerobic respiration
B0009331cellular_componentglycerol-3-phosphate dehydrogenase (FAD) complex
B0016491molecular_functionoxidoreductase activity
B0019563biological_processglycerol catabolic process
B0019637biological_processorganophosphate metabolic process
B0042803molecular_functionprotein homodimerization activity
B0046168biological_processglycerol-3-phosphate catabolic process
B0071949molecular_functionFAD binding
Functional Information from PROSITE/UniProt
site_idPS00977
Number of Residues18
DetailsFAD_G3PDH_1 FAD-dependent glycerol-3-phosphate dehydrogenase signature 1. IGGGinGAGiAaDaagRG
ChainResidueDetails
AILE9-GLY26

site_idPS00978
Number of Residues11
DetailsFAD_G3PDH_2 FAD-dependent glycerol-3-phosphate dehydrogenase signature 2. GGKltTYRklA
ChainResidueDetails
AGLY352-ALA362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AASP5
BASP5

229380

PDB entries from 2024-12-25

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