Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6POP

Crystal structure of DauA in complex with NADP+

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
E0016491molecular_functionoxidoreductase activity
E0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F0016491molecular_functionoxidoreductase activity
F0016620molecular_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 Residues30
Detailsbinding site for residue NAP A 501
ChainResidue
APHE144
AASP209
ALEU222
AILE223
AGLY224
ASER225
AVAL228
AHIS231
AGLU246
ALEU247
AGLY248
ALEU145
AGLY249
ACYS280
AGLU378
ALEU406
AHIS443
AEDO504
AHOH609
AHOH617
AHOH669
AHOH678
ATRP147
AHOH681
AASN148
ALYS171
ASER173
ASER174
AASP204
AGLY208

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 503
ChainResidue
AASN440
ALEU457

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 504
ChainResidue
ANAP501
AHOH607

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 505
ChainResidue
AILE22
APRO24
AMET323
AASP324
ATYR358
AHOH622

site_idAC5
Number of Residues34
Detailsbinding site for residue NAP B 501
ChainResidue
BPHE144
BLEU145
BALA146
BTRP147
BASN148
BLYS171
BSER173
BSER174
BASP204
BGLY208
BASP209
BLEU222
BILE223
BGLY224
BSER225
BVAL228
BHIS231
BGLU246
BLEU247
BGLY248
BGLY249
BCYS280
BGLU378
BPHE380
BHIS443
BMG503
BHOH605
BHOH615
BHOH617
BHOH627
BHOH629
BHOH641
BHOH643
BHOH661

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 502
ChainResidue
BLEU152
BTYR156
BTYR437
BHIS443

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 503
ChainResidue
BNAP501
BHOH605
BHOH615
BHOH635
BHOH643
BHOH661

site_idAC8
Number of Residues34
Detailsbinding site for residue NAP C 501
ChainResidue
CHIS231
CGLU246
CLEU247
CGLY248
CGLY249
CCYS280
CGLU378
CLEU406
CHIS443
CMG502
CHOH604
CHOH607
CHOH611
CHOH612
CHOH635
CHOH639
CHOH640
CHOH670
CHOH683
CPHE144
CLEU145
CTRP147
CASN148
CLYS171
CSER173
CSER174
CASP204
CGLY208
CASP209
CLEU222
CILE223
CGLY224
CSER225
CVAL228

site_idAC9
Number of Residues6
Detailsbinding site for residue MG C 502
ChainResidue
CNAP501
CHOH604
CHOH639
CHOH670
CHOH683
CHOH699

site_idAD1
Number of Residues32
Detailsbinding site for residue NAP D 501
ChainResidue
DPHE144
DLEU145
DTRP147
DASN148
DLYS171
DSER173
DSER174
DASP204
DGLY208
DASP209
DLEU222
DILE223
DGLY224
DSER225
DVAL228
DHIS231
DGLU246
DLEU247
DGLY248
DCYS280
DGLU378
DPHE380
DHIS443
DEDO504
DHOH604
DHOH605
DHOH611
DHOH620
DHOH623
DHOH633
DHOH665
DHOH666

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO D 502
ChainResidue
CILE122
DSER456
DLEU457
DLEU458
DHOH610

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO D 503
ChainResidue
DTYR156
DTYR437
DHOH649

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO D 504
ChainResidue
DSER225
DVAL228
DNAP501

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO D 505
ChainResidue
DTHR226
DALA404

site_idAD6
Number of Residues29
Detailsbinding site for residue NAP E 501
ChainResidue
ELEU145
EALA146
ETRP147
EASN148
ELYS171
ESER173
ESER174
EASP204
EGLY208
EASP209
ELEU222
EILE223
EGLY224
ESER225
EVAL228
EHIS231
EGLU246
ELEU247
EGLY248
EGLY249
ECYS280
EGLU378
EPHE380
EHIS443
EHOH605
EHOH625
EHOH632
EHOH636
EHOH639

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO E 502
ChainResidue
ETYR156
EVAL281
ETYR437
EHIS443

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO E 503
ChainResidue
EARG63
EILE114
EARG135

site_idAD9
Number of Residues30
Detailsbinding site for residue NAP F 501
ChainResidue
FPHE144
FLEU145
FALA146
FTRP147
FASN148
FLYS171
FSER173
FSER174
FASP204
FGLY208
FASP209
FLEU222
FILE223
FGLY224
FSER225
FVAL228
FHIS231
FGLU246
FLEU247
FGLY248
FCYS280
FGLU378
FPHE380
FHIS443
FHOH615
FHOH633
FHOH639
FHOH643
FHOH653
FHOH672

site_idAE1
Number of Residues2
Detailsbinding site for residue EDO F 502
ChainResidue
FTYR156
FHIS443

site_idAE2
Number of Residues2
Detailsbinding site for residue EDO F 503
ChainResidue
FTHR226
FASP403

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGNAP
ChainResidueDetails
AMET245-PRO252

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon