Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5TSO

CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PIG MUSCLE COMPLEXED WITH ORTHOPHENANTHROLINE AT 1.90 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
P0000226biological_processmicrotubule cytoskeleton organization
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0006417biological_processregulation of translation
P0006915biological_processapoptotic process
P0008017molecular_functionmicrotubule binding
P0015630cellular_componentmicrotubule cytoskeleton
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0016740molecular_functiontransferase activity
P0032481biological_processpositive regulation of type I interferon production
P0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
P0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
P0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
P0045087biological_processinnate immune response
P0050661molecular_functionNADP binding
P0050821biological_processprotein stabilization
P0051287molecular_functionNAD binding
P0051402biological_processneuron apoptotic process
P0097452cellular_componentGAIT complex
R0000226biological_processmicrotubule cytoskeleton organization
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005634cellular_componentnucleus
R0005737cellular_componentcytoplasm
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0006417biological_processregulation of translation
R0006915biological_processapoptotic process
R0008017molecular_functionmicrotubule binding
R0015630cellular_componentmicrotubule cytoskeleton
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0016740molecular_functiontransferase activity
R0032481biological_processpositive regulation of type I interferon production
R0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
R0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0045087biological_processinnate immune response
R0050661molecular_functionNADP binding
R0050821biological_processprotein stabilization
R0051287molecular_functionNAD binding
R0051402biological_processneuron apoptotic process
R0097452cellular_componentGAIT complex
S0000226biological_processmicrotubule cytoskeleton organization
S0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
S0005634cellular_componentnucleus
S0005737cellular_componentcytoplasm
S0005829cellular_componentcytosol
S0005856cellular_componentcytoskeleton
S0006006biological_processglucose metabolic process
S0006096biological_processglycolytic process
S0006417biological_processregulation of translation
S0006915biological_processapoptotic process
S0008017molecular_functionmicrotubule binding
S0015630cellular_componentmicrotubule cytoskeleton
S0016491molecular_functionoxidoreductase activity
S0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
S0016740molecular_functiontransferase activity
S0032481biological_processpositive regulation of type I interferon production
S0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
S0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
S0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
S0045087biological_processinnate immune response
S0050661molecular_functionNADP binding
S0050821biological_processprotein stabilization
S0051287molecular_functionNAD binding
S0051402biological_processneuron apoptotic process
S0097452cellular_componentGAIT complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 P 501
ChainResidue
PSER148
PTHR151
PTHR208
PGLY209
PALA210
PHOH619
PHOH698

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 P 502
ChainResidue
PARG231
PNAD503
PHOH691
PHOH748
PHOH780
PTHR179
PTHR181

site_idAC3
Number of Residues35
Detailsbinding site for residue NAD P 503
ChainResidue
PASN6
PGLY7
PPHE8
PGLY9
PARG10
PILE11
PASN31
PASP32
PPRO33
PPHE34
PARG77
PSER95
PTHR96
PGLY97
PSER119
PALA120
PALA180
PASN313
PTYR317
PSO4502
PHOH630
PHOH634
PHOH645
PHOH658
PHOH681
PHOH682
PHOH684
PHOH686
PHOH694
PHOH748
PHOH752
PHOH757
PHOH760
PHOH786
PHOH796

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 P 504
ChainResidue
PARG77
PHOH609
PHOH673
PHOH715

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 P 505
ChainResidue
PSER263
PLYS268
PHIS288
PHOH601

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 P 506
ChainResidue
PASN301
PASP302
PHIS303

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL P 507
ChainResidue
PTYR46
PLYS52
PTHR274
PTHR291
PHOH647
PHOH653
PHOH669

site_idAC8
Number of Residues5
Detailsbinding site for residue PHN R 401
ChainResidue
RMET130
RHIS134
RLYS268
RILE270
SGOL409

site_idAC9
Number of Residues9
Detailsbinding site for residue PHN R 402
ChainResidue
RVAL1
RLYS24
RALA329
RSER330
RGOL408
RHOH648
SGLY265
SPRO266
SHOH680

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 R 403
ChainResidue
RSER148
RTHR151
RTHR208
RGLY209
RALA210
RHOH508

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 R 404
ChainResidue
RTHR179
RTHR181
RARG231
RNAD405
RHOH522
RHOH598

site_idAD3
Number of Residues33
Detailsbinding site for residue NAD R 405
ChainResidue
RASN31
RASP32
RPRO33
RPHE34
RILE35
RGLU76
RARG77
RSER95
RTHR96
RGLY97
RSER119
RALA120
RCYS149
RALA180
RASN313
RTYR317
RSO4404
RHOH503
RHOH513
RHOH538
RHOH579
RHOH582
RHOH592
RHOH603
RHOH613
RHOH624
RHOH640
RASN6
RGLY7
RPHE8
RGLY9
RARG10
RILE11

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 R 406
ChainResidue
RGLN75
RARG77
RHOH532
RHOH555

site_idAD5
Number of Residues4
Detailsbinding site for residue SO4 R 407
ChainResidue
RASN301
RASP302
RHIS303
RHOH510

site_idAD6
Number of Residues5
Detailsbinding site for residue GOL R 408
ChainResidue
RLYS24
RPHN402
SGLY265
SPRO266
SPHN401

site_idAD7
Number of Residues6
Detailsbinding site for residue GOL R 409
ChainResidue
RTYR46
RTHR274
RPHE283
RASP286
RTHR291
RHOH512

site_idAD8
Number of Residues9
Detailsbinding site for residue PHN S 401
ChainResidue
RGOL408
SMET130
SHIS134
SPRO266
SLYS268
SILE270
SASP323
SHOH657
SHOH798

site_idAD9
Number of Residues8
Detailsbinding site for residue PHN S 402
ChainResidue
RGLY265
RPRO266
RHOH628
SVAL1
SLYS24
SALA329
SSER330
SGOL409

site_idAE1
Number of Residues9
Detailsbinding site for residue SO4 S 403
ChainResidue
SSER148
STHR208
SGLY209
SALA210
SHOH502
SHOH520
SHOH568
SHOH599
SHOH636

site_idAE2
Number of Residues8
Detailsbinding site for residue SO4 S 404
ChainResidue
STHR179
STHR181
SARG231
SNAD405
SHOH611
SHOH671
SHOH678
SHOH692

site_idAE3
Number of Residues36
Detailsbinding site for residue NAD S 405
ChainResidue
SASN6
SGLY7
SPHE8
SGLY9
SARG10
SILE11
SASN31
SASP32
SPRO33
SPHE34
SGLU76
SARG77
SSER95
STHR96
SGLY97
SSER119
SALA120
SCYS149
SALA180
SPRO188
SASN313
STYR317
SSO4404
SHOH515
SHOH556
SHOH565
SHOH571
SHOH576
SHOH578
SHOH598
SHOH620
SHOH634
SHOH668
SHOH678
SHOH686
SHOH732

site_idAE4
Number of Residues4
Detailsbinding site for residue GOL S 406
ChainResidue
SASN301
SASP302
SHIS303
SHOH609

site_idAE5
Number of Residues9
Detailsbinding site for residue GOL S 407
ChainResidue
STYR46
SLYS52
STHR274
SASP282
STHR291
SHOH516
SHOH564
SHOH629
SHOH667

site_idAE6
Number of Residues6
Detailsbinding site for residue GOL S 408
ChainResidue
SSER263
SLYS268
SHIS288
SHOH557
SHOH624
SHOH730

site_idAE7
Number of Residues7
Detailsbinding site for residue GOL S 409
ChainResidue
RGLY265
RPRO266
RPHN401
SLYS24
SPHN402
SHOH503
SHOH505

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
PALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
PCYS149
RCYS149
SCYS149

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PARG10
RASN313
SARG10
SASP32
SARG77
SSER119
SASN313
PASP32
PARG77
PSER119
PASN313
RARG10
RASP32
RARG77
RSER119

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
PSER148
STHR179
STHR208
SARG231
PTHR179
PTHR208
PARG231
RSER148
RTHR179
RTHR208
RARG231
SSER148

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PHIS176
RHIS176
SHIS176

site_idSWS_FT_FI5
Number of Residues15
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS2
RLYS331
SLYS2
SLYS63
SLYS257
SLYS260
SLYS331
PLYS63
PLYS257
PLYS260
PLYS331
RLYS2
RLYS63
RLYS257
RLYS260

site_idSWS_FT_FI6
Number of Residues21
DetailsMOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PASN6
RASN67
RASN146
RASN152
RASN222
RASN313
SASN6
SASN61
SASN67
SASN146
SASN152
PASN61
SASN222
SASN313
PASN67
PASN146
PASN152
PASN222
PASN313
RASN6
RASN61

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PTYR39
RTYR39
STYR39

site_idSWS_FT_FI8
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS58
PLYS216
PLYS251
RLYS58
RLYS216
RLYS251
SLYS58
SLYS216
SLYS251

site_idSWS_FT_FI9
Number of Residues24
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PTHR72
RTHR150
RTHR174
RTHR179
RTHR181
RTHR208
RTHR226
RTHR234
STHR72
STHR150
STHR174
PTHR150
STHR179
STHR181
STHR208
STHR226
STHR234
PTHR174
PTHR179
PTHR181
PTHR208
PTHR226
PTHR234
RTHR72

site_idSWS_FT_FI10
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PSER119
RSER238
RSER309
RSER330
SSER119
SSER145
SSER148
SSER238
SSER309
SSER330
PSER145
PSER148
PSER238
PSER309
PSER330
RSER119
RSER145
RSER148

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797
ChainResidueDetails
PCYS149
RCYS149
SCYS149

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS191
PLYS212
RLYS191
RLYS212
SLYS191
SLYS212

site_idSWS_FT_FI13
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS224
RLYS224
SLYS224

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PCYS244
RCYS244
SCYS244

site_idSWS_FT_FI15
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS183
RLYS183
SLYS183

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon