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7C5N

Crystal Structure of C150A+H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli at 2.0 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 Residues35
Detailsbinding site for residue NAD O 401
ChainResidue
OASN7
OLYS78
OCYS96
OTHR97
OGLY98
OPHE99
OSER120
OALA121
OALA150
OASN315
OPHE319
OGLY8
OCL405
OHOH507
OHOH513
OHOH564
OHOH576
OHOH581
OHOH587
OHOH601
OHOH607
OHOH609
OPHE9
OHOH612
OHOH644
OHOH661
OHOH668
OHOH669
OHOH673
OGLY10
OARG11
OILE12
OASN33
OASP34
OLEU35

site_idAC2
Number of Residues8
Detailsbinding site for residue PO4 O 402
ChainResidue
OALA201
OHOH616
OHOH636
PALA201
PHOH645
QALA201
RALA201
RHOH603

site_idAC3
Number of Residues4
Detailsbinding site for residue CL O 403
ChainResidue
OLYS227
OGLY228
OHOH733
OHOH797

site_idAC4
Number of Residues4
Detailsbinding site for residue CL O 404
ChainResidue
OALA80
OLYS81
OALA108
OHOH771

site_idAC5
Number of Residues3
Detailsbinding site for residue CL O 405
ChainResidue
OTHR180
ONAD401
OHOH646

site_idAC6
Number of Residues30
Detailsbinding site for residue NAD P 401
ChainResidue
PASN7
PGLY8
PPHE9
PGLY10
PARG11
PILE12
PASN33
PASP34
PLYS78
PCYS96
PTHR97
PGLY98
PSER120
PALA121
PALA150
PTHR180
PASN315
PPHE319
PCL404
PHOH502
PHOH523
PHOH543
PHOH597
PHOH602
PHOH610
PHOH622
PHOH629
PHOH640
PHOH655
PHOH684

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO P 402
ChainResidue
PGLU62
PHOH522

site_idAC8
Number of Residues3
Detailsbinding site for residue CL P 403
ChainResidue
PLYS227
PGLY228
PHOH775

site_idAC9
Number of Residues3
Detailsbinding site for residue CL P 404
ChainResidue
PTHR180
PNAD401
PHOH603

site_idAD1
Number of Residues4
Detailsbinding site for residue CL P 405
ChainResidue
PALA80
PLYS81
PALA108
PHOH714

site_idAD2
Number of Residues33
Detailsbinding site for residue NAD Q 401
ChainResidue
QARG11
QILE12
QASN33
QASP34
QLYS78
QCYS96
QTHR97
QGLY98
QPHE99
QSER120
QALA121
QALA150
QTHR180
QASN315
QPHE319
QCL404
QHOH519
QHOH524
QHOH552
QHOH581
QHOH584
QHOH591
QHOH596
QHOH604
QHOH615
QHOH618
QHOH621
QHOH622
QHOH641
QHOH643
QASN7
QGLY8
QGLY10

site_idAD3
Number of Residues2
Detailsbinding site for residue CL Q 402
ChainResidue
QLYS227
QGLY228

site_idAD4
Number of Residues3
Detailsbinding site for residue CL Q 403
ChainResidue
QALA80
QLYS81
QHOH716

site_idAD5
Number of Residues3
Detailsbinding site for residue CL Q 404
ChainResidue
QTHR180
QNAD401
QHOH535

site_idAD6
Number of Residues33
Detailsbinding site for residue NAD R 401
ChainResidue
RASN7
RGLY8
RPHE9
RGLY10
RARG11
RILE12
RASN33
RASP34
RLEU35
RLYS78
RCYS96
RTHR97
RGLY98
RPHE99
RSER120
RALA121
RALA150
RTHR180
RASN315
RPHE319
RHOH513
RHOH521
RHOH530
RHOH550
RHOH567
RHOH586
RHOH587
RHOH600
RHOH604
RHOH609
RHOH625
RHOH662
RHOH666

site_idAD7
Number of Residues4
Detailsbinding site for residue CL R 402
ChainResidue
QHOH571
RLYS227
RGLY228
RHOH675

site_idAD8
Number of Residues3
Detailsbinding site for residue CL R 403
ChainResidue
RTHR180
RTHR182
RHOH550

Functional Information from PROSITE/UniProt
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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