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5JYF

Structures of Streptococcus agalactiae GBS GAPDH in different enzymatic states

Functional Information from GO Data
ChainGOidnamespacecontents
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0042802molecular_functionidentical protein binding
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0006006biological_processglucose metabolic process
D0006096biological_processglycolytic process
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0042802molecular_functionidentical protein binding
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA150-LEU157

253795

PDB entries from 2026-05-20

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