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5ZU2

Effect of mutation (R554A) on FAD modification in Aspergillus oryzae RIB40formate oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0050660molecular_functionflavin adenine dinucleotide binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0050660molecular_functionflavin adenine dinucleotide binding
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues40
Detailsbinding site for residue FAD A 601
ChainResidue
AGLY14
AGLY88
ALYS89
ATHR90
AGLY93
ASER94
ASER95
AASN98
ATYR99
APHE100
ATHR101
AGLY16
AVAL228
AHIS229
ASER230
ASER266
AGLN267
AGLY268
AGLU271
APHE510
AASP543
AALA544
ATHR17
AALA554
AILE555
AGLN556
AVAL559
AHOH753
AHOH762
AHOH771
AHOH778
AHOH783
AHOH802
AALA18
AHOH854
AGLU38
AALA39
ATRP66
ATHR86
AARG87

site_idAC2
Number of Residues3
Detailsbinding site for residue MPD A 602
ChainResidue
ATYR469
AHOH711
BLYS474

site_idAC3
Number of Residues3
Detailsbinding site for residue MPD A 603
ChainResidue
AASP260
CPRO384
CASN454

site_idAC4
Number of Residues8
Detailsbinding site for residue MPD A 604
ChainResidue
AHIS408
ATRP488
APRO491
AARG500
AALA501
AASP504
AARG505
AHOH872

site_idAC5
Number of Residues9
Detailsbinding site for residue ACT A 605
ChainResidue
ATRP66
ATYR68
AHIS229
AGLU271
ALYS274
APRO441
APHE442
AGLN443
AGLN444

site_idAC6
Number of Residues39
Detailsbinding site for residue FAD B 601
ChainResidue
BHOH759
BHOH782
BHOH796
BGLY14
BGLY15
BGLY16
BTHR17
BALA18
BGLU38
BALA39
BTRP66
BTHR86
BARG87
BGLY88
BLYS89
BTHR90
BGLY93
BSER94
BASN98
BTYR99
BPHE100
BTHR101
BVAL228
BHIS229
BSER230
BSER266
BGLN267
BGLY268
BGLU271
BPHE510
BASP543
BALA544
BALA554
BILE555
BGLN556
BVAL559
BHOH730
BHOH734
BHOH751

site_idAC7
Number of Residues4
Detailsbinding site for residue MPD B 602
ChainResidue
BGLU162
BARG206
BASN344
BARG345

site_idAC8
Number of Residues36
Detailsbinding site for residue FAD C 601
ChainResidue
CGLY14
CGLY15
CGLY16
CTHR17
CALA18
CGLU38
CALA39
CTRP66
CTHR86
CARG87
CGLY88
CLYS89
CTHR90
CGLY93
CSER94
CSER95
CLEU97
CASN98
CTYR99
CPHE100
CTHR101
CVAL228
CSER230
CSER266
CGLN267
CGLY268
CGLU271
CPHE510
CASP543
CALA544
CALA554
CILE555
CGLN556
CVAL559
CHOH749
CHOH760

site_idAC9
Number of Residues4
Detailsbinding site for residue MPD C 602
ChainResidue
CTYR469
CGLU485
CLEU492
CHOH717

Functional Information from PROSITE/UniProt
site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GKtLGGSSsLNyftWvpGhkatfD
ChainResidueDetails
AGLY88-ASP111

225946

PDB entries from 2024-10-09

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