2BVF
Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | TRP31 |
| A | ALA78 |
| A | LEU88 |
| A | GLY107 |
| A | MET129 |
| A | HIS130 |
| A | VAL133 |
| A | GLY134 |
| A | CYS136 |
| A | GLY137 |
| A | LEU138 |
| A | VAL67 |
| A | LEU140 |
| A | ASN141 |
| A | GLY143 |
| A | VAL144 |
| A | PRO190 |
| A | GLY193 |
| A | VAL195 |
| A | ASN413 |
| A | HIS450 |
| A | ASN451 |
| A | ARG68 |
| A | HOH2118 |
| A | HOH2533 |
| A | HOH2540 |
| A | HOH2541 |
| A | HOH2542 |
| A | HOH2543 |
| A | HOH2544 |
| A | SER69 |
| A | GLY70 |
| A | GLY71 |
| A | HIS72 |
| A | ASN73 |
| A | TYR77 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD B 700 |
| 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 | MET129 |
| B | HIS130 |
| B | VAL133 |
| B | GLY134 |
| B | CYS136 |
| B | GLY137 |
| B | LEU138 |
| B | LEU140 |
| B | ASN141 |
| B | GLY143 |
| B | VAL144 |
| B | PRO190 |
| B | GLY193 |
| B | VAL195 |
| B | ASN413 |
| B | HIS450 |
| B | ASN451 |
| B | HOH2481 |
| B | HOH2483 |
| B | HOH2542 |
| B | HOH2543 |
| B | HOH2544 |
| B | HOH2545 |
| B | HOH2546 |
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 | 342 |
| 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 | 28 |
| 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 | 2 |
| 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 |
