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6H3O

Alcohol oxidase from Phanerochaete chrysosporium mutant F101S

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
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0050660molecular_functionflavin adenine dinucleotide binding
E0000166molecular_functionnucleotide binding
E0016491molecular_functionoxidoreductase activity
E0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
E0050660molecular_functionflavin adenine dinucleotide binding
F0000166molecular_functionnucleotide binding
F0016491molecular_functionoxidoreductase activity
F0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
F0050660molecular_functionflavin adenine dinucleotide binding
G0000166molecular_functionnucleotide binding
G0016491molecular_functionoxidoreductase activity
G0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
G0050660molecular_functionflavin adenine dinucleotide binding
H0000166molecular_functionnucleotide binding
H0016491molecular_functionoxidoreductase activity
H0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
H0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
Detailsbinding site for residue FAD A 701
ChainResidue
AGLY13
AGLY95
AGLY96
AASN100
ASER101
AGLN102
AMET103
AALA227
AARG228
AVAL229
ASER271
AGLY15
ASER272
AGLY273
AILE280
ATRP560
AHIS561
AASP593
ALEU594
AASN604
ATHR605
ATYR606
APRO16
AALA609
AHOH818
AHOH827
AHOH830
AHOH839
AALA17
AGLU38
AGLY39
AALA90
AASN91
AILE92

site_idAC2
Number of Residues34
Detailsbinding site for residue FAD B 701
ChainResidue
BGLY15
BPRO16
BALA17
BGLU38
BGLY39
BMET59
BALA90
BASN91
BILE92
BGLY95
BGLY96
BASN100
BSER101
BGLN102
BMET103
BALA227
BARG228
BVAL229
BSER272
BGLY273
BILE280
BTRP560
BHIS561
BASP593
BLEU594
BASN604
BTHR605
BTYR606
BALA609
BHOH806
BHOH813
BHOH814
BHOH824
BHOH842

site_idAC3
Number of Residues33
Detailsbinding site for residue FAD C 701
ChainResidue
CHOH850
CHOH863
CGLY13
CPRO16
CALA17
CGLU38
CGLY39
CALA90
CASN91
CILE92
CGLY95
CGLY96
CASN100
CSER101
CGLN102
CMET103
CALA227
CVAL229
CSER271
CSER272
CGLY273
CTRP560
CHIS561
CASP593
CLEU594
CASN604
CTHR605
CTYR606
CALA609
CHOH812
CHOH820
CHOH822
CHOH825

site_idAC4
Number of Residues32
Detailsbinding site for residue FAD D 701
ChainResidue
DGLY13
DGLY15
DPRO16
DALA17
DGLU38
DGLY39
DALA90
DASN91
DILE92
DGLY95
DGLY96
DASN100
DSER101
DGLN102
DMET103
DALA227
DARG228
DVAL229
DSER271
DSER272
DGLY273
DTRP560
DHIS561
DASP593
DLEU594
DASN604
DTHR605
DTYR606
DALA609
DHOH807
DHOH831
DHOH841

site_idAC5
Number of Residues31
Detailsbinding site for residue FAD E 701
ChainResidue
EGLY13
EGLY15
EPRO16
EALA17
EGLU38
EGLY39
EALA90
EASN91
EILE92
EGLY95
EGLY96
EASN100
ESER101
EGLN102
EMET103
EALA227
EARG228
EVAL229
ESER272
ETRP560
EHIS561
EASP593
ELEU594
EASN604
ETHR605
ETYR606
EALA609
EHOH802
EHOH805
EHOH816
EHOH825

site_idAC6
Number of Residues32
Detailsbinding site for residue FAD F 701
ChainResidue
FGLY13
FGLY15
FPRO16
FGLU38
FGLY39
FMET59
FALA90
FASN91
FILE92
FGLY95
FGLY96
FASN100
FSER101
FGLN102
FMET103
FALA227
FARG228
FVAL229
FSER272
FGLY273
FILE280
FTRP560
FHIS561
FASP593
FLEU594
FASN604
FTHR605
FTYR606
FALA609
FHOH801
FHOH818
FHOH856

site_idAC7
Number of Residues31
Detailsbinding site for residue FAD G 701
ChainResidue
GGLY13
GGLY15
GPRO16
GALA17
GGLU38
GGLY39
GALA90
GASN91
GILE92
GGLY95
GGLY96
GASN100
GSER101
GGLN102
GMET103
GALA227
GARG228
GVAL229
GSER271
GSER272
GGLY273
GILE280
GTRP560
GHIS561
GASP593
GLEU594
GASN604
GTHR605
GTYR606
GALA609
GHOH811

site_idAC8
Number of Residues32
Detailsbinding site for residue FAD H 701
ChainResidue
HGLY13
HGLY15
HPRO16
HGLU38
HGLY39
HALA90
HASN91
HILE92
HGLY95
HGLY96
HASN100
HSER101
HGLN102
HMET103
HALA227
HARG228
HVAL229
HSER272
HGLY273
HILE280
HTRP560
HHIS561
HLEU594
HASN604
HTHR605
HTYR606
HALA609
HHOH801
HHOH811
HHOH818
HHOH866
HHOH872

site_idAC9
Number of Residues1
Detailsbinding site for residue GOL H 702
ChainResidue
HTYR442

Functional Information from PROSITE/UniProt
site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. ANiLGGGSsINsqmYtrAsasdwD
ChainResidueDetails
AALA90-ASP113

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GTlgTPqILerSGVG
ChainResidueDetails
AGLY273-GLY287

221051

PDB entries from 2024-06-12

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