2BVH
Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009820 | biological_process | alkaloid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018530 | molecular_function | (R)-6-hydroxynicotine oxidase activity |
| A | 0019608 | biological_process | nicotine catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009820 | biological_process | alkaloid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018530 | molecular_function | (R)-6-hydroxynicotine oxidase activity |
| B | 0019608 | biological_process | nicotine catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009820 | biological_process | alkaloid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018530 | molecular_function | (R)-6-hydroxynicotine oxidase activity |
| C | 0019608 | biological_process | nicotine catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009820 | biological_process | alkaloid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018530 | molecular_function | (R)-6-hydroxynicotine oxidase activity |
| D | 0019608 | biological_process | nicotine catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | TRP31 |
| A | ALA78 |
| A | LEU88 |
| A | GLY107 |
| A | GLY128 |
| A | MET129 |
| A | HIS130 |
| A | VAL133 |
| A | GLY134 |
| A | CYS136 |
| A | GLY137 |
| A | VAL67 |
| A | LEU138 |
| A | GLY143 |
| A | VAL144 |
| A | PRO190 |
| A | GLY193 |
| A | VAL195 |
| A | ASN413 |
| A | HIS450 |
| A | ASN451 |
| A | ARG68 |
| A | SER69 |
| A | GLY70 |
| A | GLY71 |
| A | HIS72 |
| A | ASN73 |
| A | TYR77 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 600 |
| Chain | Residue |
| B | TRP31 |
| B | VAL67 |
| B | ARG68 |
| B | SER69 |
| B | GLY70 |
| B | GLY71 |
| B | HIS72 |
| B | ASN73 |
| B | TYR77 |
| B | ALA78 |
| B | LEU88 |
| B | GLY107 |
| B | GLY128 |
| B | MET129 |
| B | HIS130 |
| B | VAL133 |
| B | GLY134 |
| B | CYS136 |
| B | GLY137 |
| B | LEU138 |
| B | GLY143 |
| B | VAL144 |
| B | PRO190 |
| B | GLY193 |
| B | VAL195 |
| B | ASN413 |
| B | HIS450 |
| B | ASN451 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD C 600 |
| Chain | Residue |
| C | TRP31 |
| C | VAL67 |
| C | ARG68 |
| C | SER69 |
| C | GLY70 |
| C | GLY71 |
| C | HIS72 |
| C | ASN73 |
| C | TYR77 |
| C | ALA78 |
| C | LEU88 |
| C | GLY107 |
| C | GLY128 |
| C | MET129 |
| C | HIS130 |
| C | VAL133 |
| C | GLY134 |
| C | CYS136 |
| C | GLY137 |
| C | LEU138 |
| C | GLY143 |
| C | VAL144 |
| C | PRO190 |
| C | GLY193 |
| C | VAL195 |
| C | ASN413 |
| C | HIS450 |
| C | ASN451 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD D 600 |
| Chain | Residue |
| D | VAL133 |
| D | GLY134 |
| D | CYS136 |
| D | GLY137 |
| D | LEU138 |
| D | GLY143 |
| D | VAL144 |
| D | PRO190 |
| D | GLY193 |
| D | VAL195 |
| D | ASN413 |
| D | HIS450 |
| D | ASN451 |
| D | TRP31 |
| D | VAL67 |
| D | ARG68 |
| D | SER69 |
| D | GLY70 |
| D | GLY71 |
| D | HIS72 |
| D | ASN73 |
| D | TYR77 |
| D | ALA78 |
| D | LEU88 |
| D | GLY107 |
| D | GLY128 |
| D | MET129 |
| D | HIS130 |
Functional Information from PROSITE/UniProt
| site_id | PS00862 |
| Number of Residues | 34 |
| Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PsliarclSagDVaksVryacdngle...IsvrSGGH |
| Chain | Residue | Details |
| A | PRO39-HIS72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 684 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16095622","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BVG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BVH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Pros-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"16095622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2115879","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2680607","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
