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1CRW

CRYSTAL STRUCTURE OF APO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR AT 2.0A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
G0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
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
R0005829cellular_componentcytosol
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 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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761850
ChainResidueDetails
GARG10
GASP32
GASN313
RARG10
RASP32
RASN313

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
GMET77
RARG231
GSER148
GTHR179
GTHR208
GARG231
RMET77
RSER148
RTHR179
RTHR208

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:0000250|UniProtKB:P00357
ChainResidueDetails
GSER1
RSER1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
GCYS149
GHIS176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RCYS149
RHIS176

site_idMCSA1
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
GCYS149covalent catalysis, proton shuttle (general acid/base)
GHIS176proton shuttle (general acid/base)

site_idMCSA2
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
RCYS149covalent catalysis, proton shuttle (general acid/base)
RHIS176proton shuttle (general acid/base)

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PDB entries from 2024-07-31

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