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5GTL

NADPH complex structure of Aldehyde Dehydrogenase from Bacillus cereus

Replaces:  4PT3
Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 501
ChainResidue
ATHR39
ATYR40
AASP108
AGLN195
AHOH647
AHOH665

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 502
ChainResidue
BILE260
BHOH914
ALYS467
AGLY470
AHOH801

site_idAC3
Number of Residues32
Detailsbinding site for residue NDP A 503
ChainResidue
AILE164
AILE165
APRO166
ATRP167
AASN168
ALYS191
AALA193
AGLU194
AGLN195
AGLY222
AGLY224
AGLY228
AALA229
APHE242
AGLY244
ASER245
ATHR248
ATYR251
AGLU266
ALEU267
ACYS300
AGLN347
AARG350
AGLU397
APHE399
AHOH602
AHOH609
AHOH651
AHOH659
AHOH660
AHOH687
AHOH848

site_idAC4
Number of Residues6
Detailsbinding site for residue NA B 501
ChainResidue
BTHR39
BTYR40
BASP108
BGLN195
BHOH638
BHOH777

site_idAC5
Number of Residues5
Detailsbinding site for residue NA B 502
ChainResidue
AILE260
AHOH633
AHOH972
BLYS467
BGLY470

site_idAC6
Number of Residues31
Detailsbinding site for residue NDP B 503
ChainResidue
BILE165
BPRO166
BTRP167
BASN168
BLYS191
BALA193
BGLU194
BGLN195
BGLY222
BGLY224
BGLY228
BALA229
BPHE242
BGLY244
BSER245
BTHR248
BTYR251
BGLU266
BLEU267
BCYS300
BLYS346
BGLN347
BARG350
BGLU397
BPHE399
BHOH601
BHOH603
BHOH609
BHOH753
BHOH819
BHOH846

site_idAC7
Number of Residues5
Detailsbinding site for residue NA C 501
ChainResidue
CLYS467
CGLY470
DILE260
DHOH619
DHOH851

site_idAC8
Number of Residues5
Detailsbinding site for residue NA C 502
ChainResidue
CTHR39
CTYR40
CASP108
CGLN195
CHOH648

site_idAC9
Number of Residues33
Detailsbinding site for residue NDP C 503
ChainResidue
CLYS191
CALA193
CGLU194
CGLN195
CGLY222
CPHE223
CGLY224
CGLY228
CALA229
CPHE242
CGLY244
CSER245
CTHR248
CTYR251
CGLU266
CLEU267
CGLY268
CCYS300
CLYS346
CGLN347
CARG350
CGLU397
CPHE399
CHOH619
CHOH621
CHOH624
CHOH664
CHOH675
CHOH798
CILE164
CILE165
CPRO166
CTRP167

site_idAD1
Number of Residues7
Detailsbinding site for residue NA D 501
ChainResidue
DTHR39
DTYR40
DASP108
DGLN195
DHOH601
DHOH646
DHOH813

site_idAD2
Number of Residues32
Detailsbinding site for residue NDP D 502
ChainResidue
DILE164
DILE165
DPRO166
DTRP167
DASN168
DMET173
DLYS191
DALA193
DGLU194
DGLN195
DGLY222
DPHE223
DGLY224
DGLY228
DALA229
DPHE242
DTHR243
DGLY244
DSER245
DTHR248
DTYR251
DGLU266
DLEU267
DCYS300
DGLN347
DARG350
DGLU397
DPHE399
DHOH609
DHOH665
DHOH732
DHOH817

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU265-PRO272

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PDB entries from 2024-07-10

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