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1GPD

STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
G0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
G0005737cellular_componentcytoplasm
G0006006biological_processglucose metabolic process
G0006096biological_processglycolytic process
G0016491molecular_functionoxidoreductase activity
G0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G0050661molecular_functionNADP binding
G0051287molecular_functionNAD binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005737cellular_componentcytoplasm
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idABG
Number of Residues6
DetailsRESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR
ChainResidue
GASN6
GASN31
GASP32
GPHE34
GTHR96
GPHE99

site_idABR
Number of Residues6
DetailsRESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR
ChainResidue
RPHE34
RTHR96
RPHE99
RASN6
RASN31
RASP32

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NAD G 335
ChainResidue
GGLY7
GPHE8
GGLY9
GARG10
GILE11
GASP32
GPHE34
GILE35
GPHE99
GSER119
GGLU314

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NAD R 339
ChainResidue
RPHE8
RARG10
RASP32
RTHR96
RPHE99
RSER119
RALA120
RCYS149
RASN313
RTYR317

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PO4 R 337
ChainResidue
RTHR179

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 R 338
ChainResidue
RTHR150
RTHR208
RGLY209

site_idAPG
Number of Residues2
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
GARG10
GALA180

site_idAPR
Number of Residues2
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
RARG10
RALA180

site_idARG
Number of Residues3
DetailsRESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR
ChainResidue
GGLY7
GASP32
RPRO188

site_idARR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR
ChainResidue
RGLY7
RPHE8
RASP32
GPRO188

site_idNBG
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NAD COFACTOR
ChainResidue
GILE11
GCYS149
GASN313
GTYR317

site_idNBR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NAD COFACTOR
ChainResidue
RILE11
RCYS149
RASN313
RTYR317

site_idNPG
Number of Residues1
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
GILE11

site_idNPR
Number of Residues1
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
RILE11

site_idNRG
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
GTHR96
GGLY97
GSER119
GALA120

site_idNRR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
ChainResidue
RTHR96
RGLY97
RSER119
RALA120

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
GALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
GCYS149
RCYS149

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:127793
ChainResidueDetails
GSER119
GASN313
RARG10
RASP32
RSER119
RASN313
GARG10
GASP32

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
RSER148
RTHR179
RTHR208
RARG231
GARG231
GSER148
GTHR179
GTHR208

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Activates thiol group during catalysis
ChainResidueDetails
GHIS176
RHIS176

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:4294736
ChainResidueDetails
GSER1
RSER1

218500

PDB entries from 2024-04-17

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