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8QMS

Succinic semialdehyde dehydrogenase from E. coli with Q262R substitution and bound NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
A0006099biological_processtricarboxylic acid cycle
A0006527biological_processL-arginine catabolic process
A0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
A0009447biological_processputrescine catabolic process
A0009450biological_processgamma-aminobutyric acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
A0042803molecular_functionprotein homodimerization activity
A0070458biological_processcellular detoxification of nitrogen compound
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
B0006099biological_processtricarboxylic acid cycle
B0006527biological_processL-arginine catabolic process
B0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
B0009447biological_processputrescine catabolic process
B0009450biological_processgamma-aminobutyric acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
B0042803molecular_functionprotein homodimerization activity
B0070458biological_processcellular detoxification of nitrogen compound
C0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
C0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
C0006099biological_processtricarboxylic acid cycle
C0006527biological_processL-arginine catabolic process
C0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
C0009447biological_processputrescine catabolic process
C0009450biological_processgamma-aminobutyric acid catabolic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
C0042803molecular_functionprotein homodimerization activity
C0070458biological_processcellular detoxification of nitrogen compound
D0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
D0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
D0006099biological_processtricarboxylic acid cycle
D0006527biological_processL-arginine catabolic process
D0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
D0009447biological_processputrescine catabolic process
D0009450biological_processgamma-aminobutyric acid catabolic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
D0042803molecular_functionprotein homodimerization activity
D0070458biological_processcellular detoxification of nitrogen compound
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YrNTGQVCAAAK
ChainResidueDetails
ATYR261-LYS272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25526","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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