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2BVF

Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0009820biological_processalkaloid metabolic process
A0016491molecular_functionoxidoreductase activity
A0018530molecular_function(R)-6-hydroxynicotine oxidase activity
A0019608biological_processnicotine catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0009820biological_processalkaloid metabolic process
B0016491molecular_functionoxidoreductase activity
B0018530molecular_function(R)-6-hydroxynicotine oxidase activity
B0019608biological_processnicotine catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
ATRP31
AALA78
ALEU88
AGLY107
AMET129
AHIS130
AVAL133
AGLY134
ACYS136
AGLY137
ALEU138
AVAL67
ALEU140
AASN141
AGLY143
AVAL144
APRO190
AGLY193
AVAL195
AASN413
AHIS450
AASN451
AARG68
AHOH2118
AHOH2533
AHOH2540
AHOH2541
AHOH2542
AHOH2543
AHOH2544
ASER69
AGLY70
AGLY71
AHIS72
AASN73
ATYR77

site_idAC2
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD B 700
ChainResidue
BTRP31
BVAL67
BARG68
BSER69
BGLY70
BGLY71
BHIS72
BASN73
BTYR77
BALA78
BLEU88
BGLY107
BMET129
BHIS130
BVAL133
BGLY134
BCYS136
BGLY137
BLEU138
BLEU140
BASN141
BGLY143
BVAL144
BPRO190
BGLY193
BVAL195
BASN413
BHIS450
BASN451
BHOH2481
BHOH2483
BHOH2542
BHOH2543
BHOH2544
BHOH2545
BHOH2546

Functional Information from PROSITE/UniProt
site_idPS00862
Number of Residues34
DetailsOX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PsliarclSagDVaksVryacdngle...IsvrSGGH
ChainResidueDetails
APRO39-HIS72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:16095622, ECO:0007744|PDB:2BVF, ECO:0007744|PDB:2BVG, ECO:0007744|PDB:2BVH
ChainResidueDetails
AVAL67
BGLY134
BVAL144
BVAL195
BASN413
BHIS450
AMET129
AGLY134
AVAL144
AVAL195
AASN413
AHIS450
BVAL67
BMET129

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Pros-8alpha-FAD histidine => ECO:0000269|PubMed:16095622, ECO:0000269|PubMed:2115879, ECO:0000269|PubMed:2680607
ChainResidueDetails
AGLY71
BGLY71

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PDB entries from 2024-09-25

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