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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3JZ4

Crystal structure of E. coli NADP dependent enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
A0005829cellular_componentcytosol
A0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
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
A0032991cellular_componentprotein-containing complex
A0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0051289biological_processprotein homotetramerization
A0102810molecular_functionglutarate-semialdehyde dehydrogenase (NADP+) activity
A1990748biological_processcellular detoxification
B0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
B0005829cellular_componentcytosol
B0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
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
B0032991cellular_componentprotein-containing complex
B0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
B0042802molecular_functionidentical protein binding
B0050661molecular_functionNADP binding
B0051289biological_processprotein homotetramerization
B0102810molecular_functionglutarate-semialdehyde dehydrogenase (NADP+) activity
B1990748biological_processcellular detoxification
C0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
C0005829cellular_componentcytosol
C0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
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
C0032991cellular_componentprotein-containing complex
C0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
C0042802molecular_functionidentical protein binding
C0050661molecular_functionNADP binding
C0051289biological_processprotein homotetramerization
C0102810molecular_functionglutarate-semialdehyde dehydrogenase (NADP+) activity
C1990748biological_processcellular detoxification
D0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
D0005829cellular_componentcytosol
D0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
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
D0032991cellular_componentprotein-containing complex
D0036243molecular_functionsuccinate-semialdehyde dehydrogenase (NADP+) activity
D0042802molecular_functionidentical protein binding
D0050661molecular_functionNADP binding
D0051289biological_processprotein homotetramerization
D0102810molecular_functionglutarate-semialdehyde dehydrogenase (NADP+) activity
D1990748biological_processcellular detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAP A 482
ChainResidue
ATHR153
AGLY216
APHE230
ATHR231
AGLY232
ASER233
AILE236
AGLU254
ALEU255
ACYS288
ALYS338
APRO154
AGLU385
APHE387
AHOH496
AHOH520
AHOH543
AHOH580
AHOH611
AHOH616
ATRP155
AASN156
ALYS179
AALA181
ASER182
AGLY210
AALA212
site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP B 482
ChainResidue
BILE152
BTHR153
BPRO154
BTRP155
BASN156
BLYS179
BALA181
BSER182
BALA212
BGLY216
BPHE230
BGLY232
BSER233
BILE236
BGLU254
BLEU255
BCYS288
BLYS338
BGLU385
BPHE387
BHOH499
BHOH523
BHOH536
BHOH609
site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP C 482
ChainResidue
CTHR153
CPRO154
CTRP155
CASN156
CLYS179
CALA181
CSER182
CGLY210
CALA212
CGLY216
CPHE230
CTHR231
CGLY232
CSER233
CILE236
CLEU255
CCYS288
CLYS338
CGLU385
CPHE387
CHOH487
site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAP D 482
ChainResidue
DILE152
DPRO154
DTRP155
DASN156
DLYS179
DALA181
DSER182
DGLY210
DSER211
DALA212
DGLY213
DGLY216
DPHE230
DTHR231
DGLY232
DSER233
DILE236
DGLU254
DLEU255
DCYS288
DLYS338
DGLU385
DPHE387
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FrNAGQTCVCAN
ChainResidueDetails
APHE281-ASN292
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNAP
ChainResidueDetails
ALEU253-PRO260
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20174634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20174634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20174634","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-07-30

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