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6J76

Structure of 3,6-anhydro-L-galactose Dehydrogenase in Complex with NAP

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
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue NAP A 501
ChainResidue
AILE146
AGLY206
AGLY210
ATHR225
AGLY226
ASER227
AALA230
ASER233
AGLU248
ALEU249
AGLY250
ATHR147
ACYS282
AGLU383
APHE385
ALEU411
AHIS449
AHOH613
AHOH616
AHOH696
AHOH728
AHOH750
AALA148
AHOH757
ATRP149
AASN150
ALYS173
ATHR175
ASER176
AGLY204

site_idAC2
Number of Residues34
Detailsbinding site for residue NAP B 501
ChainResidue
BILE146
BTHR147
BALA148
BTRP149
BASN150
BLYS173
BTHR175
BSER176
BGLY204
BGLY206
BARG207
BGLY210
BASN211
BTHR225
BGLY226
BSER227
BALA230
BSER233
BGLU248
BLEU249
BCYS282
BGLU383
BPHE385
BLEU411
BHIS449
BHOH608
BHOH614
BHOH618
BHOH636
BHOH656
BHOH666
BHOH687
BHOH700
BHOH766

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdNCGQVCTCNE
ChainResidueDetails
APHE275-GLU286

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP
ChainResidueDetails
ALEU247-PRO254

226707

PDB entries from 2024-10-30

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