7ZQK

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

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0005515	molecular_function	protein binding
O	0006006	biological_process	glucose metabolic process
O	0009507	cellular_component	chloroplast
O	0016491	molecular_function	oxidoreductase activity
O	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O	0019253	biological_process	reductive pentose-phosphate cycle
O	0019900	molecular_function	kinase binding
O	0042802	molecular_function	identical protein binding
O	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
O	0050661	molecular_function	NADP binding
O	0051287	molecular_function	NAD binding
R	0005515	molecular_function	protein binding
R	0006006	biological_process	glucose metabolic process
R	0009507	cellular_component	chloroplast
R	0016491	molecular_function	oxidoreductase activity
R	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R	0019253	biological_process	reductive pentose-phosphate cycle
R	0019900	molecular_function	kinase binding
R	0042802	molecular_function	identical protein binding
R	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
R	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL

Chain	Residue	Details
O	ALA147-LEU154

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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