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6PNU

Crystal structure of native DauA

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 Residues2
Detailsbinding site for residue EDO A 501
ChainResidue
AARG63
AARG135

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 502
ChainResidue
AARG426
AHOH656
CVAL138
CSER218

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
ATRP93
BTRP93
BLYS313
AGLU78
AGLN79
AARG82

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO B 501
ChainResidue
AGLN79
ATRP93
ALYS313
BARG82
BTRP93
BGLN94

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO B 502
ChainResidue
BILE38
BTHR206
CTYR358

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO B 503
ChainResidue
BASN400
BHOH622

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 504
ChainResidue
BLYS171
BASP204
BGLY208
BVAL228
BHOH620
BHOH765

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO B 505
ChainResidue
BPHE380
BHOH621

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 506
ChainResidue
BLEU152
BTYR156
BCYS280
BHIS443
BHOH612

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO C 501
ChainResidue
CASN440
CSER456
CLEU457
CHOH721

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO C 502
ChainResidue
CGLN394
CSER397
CASP398
CASP401

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO C 503
ChainResidue
CARG82
CTRP93
CHOH653
DTRP93
DLYS313
DASN314

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO C 504
ChainResidue
CASP324
CALA325
CASN326

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO C 505
ChainResidue
CTYR156
CCYS280
CVAL281
CTYR437
CHIS443

site_idAD6
Number of Residues6
Detailsbinding site for residue EDO D 501
ChainResidue
BPRO137
BVAL138
BALA465
DARG426
DILE446
DLYS447

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO D 502
ChainResidue
DTHR226
DGLY248
DGLN448
DHOH624

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO D 503
ChainResidue
DGLN94
DSER95
DALA274
DASP318

site_idAD9
Number of Residues1
Detailsbinding site for residue EDO D 504
ChainResidue
DLYS305

site_idAE1
Number of Residues3
Detailsbinding site for residue EDO D 505
ChainResidue
DLEU152
DTYR156
DHIS443

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO D 506
ChainResidue
BVAL138
BSER218
DLYS447
DGLN448

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

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PDB entries from 2024-07-17

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