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7ZQK

Crystal structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii (CrGAPA) complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005515molecular_functionprotein binding
O0005829cellular_componentcytosol
O0006006biological_processglucose metabolic process
O0009507cellular_componentchloroplast
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0019253biological_processreductive pentose-phosphate cycle
O0019900molecular_functionkinase binding
O0042802molecular_functionidentical protein binding
O0047100molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
O0048046cellular_componentapoplast
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
O0099080cellular_componentsupramolecular complex
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005515molecular_functionprotein binding
R0005829cellular_componentcytosol
R0006006biological_processglucose metabolic process
R0009507cellular_componentchloroplast
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0019253biological_processreductive pentose-phosphate cycle
R0019900molecular_functionkinase binding
R0042802molecular_functionidentical protein binding
R0047100molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
R0048046cellular_componentapoplast
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
R0099080cellular_componentsupramolecular complex
Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
OCYS149
RCYS149

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
OARG77
OSER148
OTHR179
OARG195
OTHR208
OARG231
OASN313
RARG10
RASP32
RARG77
RSER148
RTHR179
RARG195
RTHR208
RARG231
RASN313
OARG10
OASP32

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000250
ChainResidueDetails
OHIS176
RHIS176

219869

PDB entries from 2024-05-15

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