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7C5O

Crystal Structure of H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with NAD at 1.98 Angstrom resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
O0000166molecular_functionnucleotide binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005737cellular_componentcytoplasm
O0006006biological_processglucose metabolic process
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0042802molecular_functionidentical protein binding
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0000166molecular_functionnucleotide binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005737cellular_componentcytoplasm
P0006006biological_processglucose metabolic process
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0042802molecular_functionidentical protein binding
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Q0000166molecular_functionnucleotide binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005737cellular_componentcytoplasm
Q0006006biological_processglucose metabolic process
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0042802molecular_functionidentical protein binding
Q0050661molecular_functionNADP binding
Q0051287molecular_functionNAD binding
R0000166molecular_functionnucleotide binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005737cellular_componentcytoplasm
R0006006biological_processglucose metabolic process
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0042802molecular_functionidentical protein binding
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue NAD O 401
ChainResidue
OASN7
OLYS78
OCYS96
OTHR97
OGLY98
OPHE99
OSER120
OALA121
OCYS150
OASN315
OPHE319
OGLY8
OHOH511
OHOH514
OHOH524
OHOH594
OHOH633
OHOH653
OHOH656
OHOH667
OHOH677
OHOH690
OPHE9
OHOH694
OHOH708
OGLY10
OARG11
OILE12
OASN33
OASP34
OLEU35

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 O 402
ChainResidue
OALA201
OHOH574
PALA201
QALA201
RALA201
RHOH610

site_idAC3
Number of Residues3
Detailsbinding site for residue CL O 403
ChainResidue
OLYS213
OLYS227
OGLY228

site_idAC4
Number of Residues6
Detailsbinding site for residue CL O 404
ChainResidue
OALA80
OLYS81
OALA108
OHOH582
OHOH768
OHOH820

site_idAC5
Number of Residues31
Detailsbinding site for residue NAD P 401
ChainResidue
PASN7
PGLY8
PPHE9
PGLY10
PARG11
PILE12
PASN33
PASP34
PLYS78
PCYS96
PTHR97
PGLY98
PPHE99
PSER120
PALA121
PCYS150
PASN315
PPHE319
PHOH502
PHOH508
PHOH512
PHOH591
PHOH602
PHOH616
PHOH620
PHOH628
PHOH631
PHOH634
PHOH653
PHOH695
QHOH562

site_idAC6
Number of Residues4
Detailsbinding site for residue CL P 402
ChainResidue
PLYS213
PLYS227
PGLY228
PHOH775

site_idAC7
Number of Residues31
Detailsbinding site for residue NAD Q 401
ChainResidue
QHOH537
QHOH548
QHOH567
QHOH574
QHOH585
QHOH607
QHOH618
QHOH620
QHOH633
QHOH648
QHOH674
QHOH678
QHOH679
QASN7
QGLY8
QGLY10
QARG11
QILE12
QASN33
QASP34
QLEU35
QLYS78
QCYS96
QTHR97
QGLY98
QPHE99
QSER120
QALA121
QCYS150
QASN315
QPHE319

site_idAC8
Number of Residues3
Detailsbinding site for residue CL Q 402
ChainResidue
QLYS227
QGLY228
QHOH774

site_idAC9
Number of Residues27
Detailsbinding site for residue NAD R 401
ChainResidue
RGLY8
RGLY10
RARG11
RILE12
RASP34
RLEU35
RLYS78
RCYS96
RTHR97
RGLY98
RPHE99
RSER120
RALA121
RCYS150
RASN315
RPHE319
RHOH512
RHOH520
RHOH537
RHOH539
RHOH544
RHOH570
RHOH573
RHOH584
RHOH605
RHOH607
RHOH632

site_idAD1
Number of Residues2
Detailsbinding site for residue CL R 402
ChainResidue
RLYS227
RGLY228

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA148-LEU155

site_idPS00430
Number of Residues89
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. hhhhhhssglvprgshmasmskvgingfgrigrlvlrrllevksnidvvaindltspkilayllkhdsnygpfpwsvdfte..................................DSLIVDGK
ChainResidueDetails
OHIS-18-LYS70

221051

PDB entries from 2024-06-12

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