Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7ZQK

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

Functional Information from GO Data
ChainGOidnamespacecontents
O0005515molecular_functionprotein binding
O0006006biological_processglucose metabolic process
O0009507cellular_componentchloroplast
O0009536cellular_componentplastid
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
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
O0099080cellular_componentsupramolecular complex
R0005515molecular_functionprotein binding
R0006006biological_processglucose metabolic process
R0009507cellular_componentchloroplast
R0009536cellular_componentplastid
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
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
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon