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2VOU

Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacter nicotinovorans

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0018663molecular_function2,6-dihydroxypyridine 3-monooxygenase activity
A0019608biological_processnicotine catabolic process
A0042803molecular_functionprotein homodimerization activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0018663molecular_function2,6-dihydroxypyridine 3-monooxygenase activity
B0019608biological_processnicotine catabolic process
B0042803molecular_functionprotein homodimerization activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0071949molecular_functionFAD binding
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0018663molecular_function2,6-dihydroxypyridine 3-monooxygenase activity
C0019608biological_processnicotine catabolic process
C0042803molecular_functionprotein homodimerization activity
C0050660molecular_functionflavin adenine dinucleotide binding
C0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues35
DetailsBINDING SITE FOR RESIDUE FAD A1395
ChainResidue
AGLY12
AVAL49
ALYS118
ACYS119
ALEU120
AALA148
AASP149
AGLY150
AVAL154
AARG173
AGLN222
ASER14
AGLY305
AASP306
AALA316
AALA317
AGLY318
AGLY319
AALA320
AGOL1396
AACT1397
AHOH2065
AILE15
AHOH2067
AHOH2187
AHOH2188
AHOH2189
AHOH2190
AHOH2191
ASER16
ATYR34
AGLU35
AARG36
ALEU41
AILE48

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1396
ChainResidue
ATYR206
AGLN222
ATYR224
APRO313
AFAD1395
AHOH2192

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A1397
ChainResidue
APRO311
AARG312
APRO313
AALA316
AALA317
AGLY318
ATYR357
AFAD1395
AHOH2159

site_idAC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD B1389
ChainResidue
BVAL11
BGLY12
BSER14
BILE15
BSER16
BTYR34
BGLU35
BARG36
BLEU41
BILE48
BVAL49
BLYS118
BCYS119
BLEU120
BALA148
BASP149
BGLY150
BVAL154
BGLN222
BASP306
BALA316
BALA317
BGLY318
BGLY319
BALA320
BGOL1390
BACT1391
BHOH2034
BHOH2125
BHOH2126
BHOH2127

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B1390
ChainResidue
BTYR206
BGLN222
BTYR224
BPRO313
BFAD1389
BHOH2110

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B1391
ChainResidue
BARG312
BPRO313
BALA316
BALA317
BGLY318
BTYR357
BFAD1389
BHOH2109

site_idAC7
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD C1389
ChainResidue
CSER16
CTYR34
CGLU35
CARG36
CLEU41
CILE48
CVAL49
CLYS118
CCYS119
CLEU120
CASP149
CGLY150
CVAL154
CGLN222
CGLY305
CASP306
CALA316
CALA317
CGLY318
CGLY319
CALA320
CGOL1390
CACT1391
CHOH2022
CHOH2066
CHOH2067
CHOH2068
CVAL11
CGLY12
CSER14
CILE15

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C1390
ChainResidue
CTYR206
CGLN222
CTYR224
CPRO313
CALA316
CFAD1389
CHOH2033

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT C1391
ChainResidue
CPRO311
CARG312
CPRO313
CALA316
CALA317
CGLY318
CTYR357
CFAD1389
CHOH2056

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:18440023
ChainResidueDetails
ASER14
BLEU120
BASP306
BALA316
CSER14
CGLU35
CVAL49
CLEU120
CASP306
CALA316
AGLU35
AVAL49
ALEU120
AASP306
AALA316
BSER14
BGLU35
BVAL49

219869

PDB entries from 2024-05-15

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