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2X5J

Crystal structure of the Apoform of the D-Erythrose-4-phosphate dehydrogenase from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0006006biological_processglucose metabolic process
O0008615biological_processpyridoxine biosynthetic process
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0042823biological_processpyridoxal phosphate biosynthetic process
O0048001molecular_functionerythrose-4-phosphate dehydrogenase activity
O0051287molecular_functionNAD binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0006006biological_processglucose metabolic process
P0008615biological_processpyridoxine biosynthetic process
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0042823biological_processpyridoxal phosphate biosynthetic process
P0048001molecular_functionerythrose-4-phosphate dehydrogenase activity
P0051287molecular_functionNAD binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005737cellular_componentcytoplasm
Q0005829cellular_componentcytosol
Q0006006biological_processglucose metabolic process
Q0008615biological_processpyridoxine biosynthetic process
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0042823biological_processpyridoxal phosphate biosynthetic process
Q0048001molecular_functionerythrose-4-phosphate dehydrogenase activity
Q0051287molecular_functionNAD binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005737cellular_componentcytoplasm
R0005829cellular_componentcytosol
R0006006biological_processglucose metabolic process
R0008615biological_processpyridoxine biosynthetic process
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0042823biological_processpyridoxal phosphate biosynthetic process
R0048001molecular_functionerythrose-4-phosphate dehydrogenase activity
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 O 1600
ChainResidue
OTHR150
OHIS176
OTHR208
OLYS209
OHOH2136

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 P 1600
ChainResidue
PLEU210
PHOH2109
PTHR150
PHIS176
PTHR208
PLYS209

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 Q 1600
ChainResidue
QTHR150
QHIS176
QTHR208
QLYS209
QHOH2097
QHOH2146

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 R 1600
ChainResidue
RTHR150
RHIS176
RTHR208
RLYS209
RLEU210
RHOH2145
RHOH2146
RHOH2147
RHOH2148

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcI
ChainResidueDetails
OALA147-ILE154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
OCYS149
PCYS149
QCYS149
RCYS149

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
OARG10
RARG10
RARG77
RASN313
OARG77
OASN313
PARG10
PARG77
PASN313
QARG10
QARG77
QASN313

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
OSER148
QARG195
QTHR208
QARG231
RSER148
RARG195
RTHR208
RARG231
OARG195
OTHR208
OARG231
PSER148
PARG195
PTHR208
PARG231
QSER148

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000250
ChainResidueDetails
OHIS176
PHIS176
QHIS176
RHIS176

222036

PDB entries from 2024-07-03

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