3K7T
Crystal structure of apo-form 6-hydroxy-L-nicotine oxidase, crystal form P3121
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0009820 | biological_process | alkaloid metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018531 | molecular_function | (S)-6-hydroxynicotine oxidase activity |
A | 0019608 | biological_process | nicotine catabolic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0009820 | biological_process | alkaloid metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018531 | molecular_function | (S)-6-hydroxynicotine oxidase activity |
B | 0019608 | biological_process | nicotine catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD A 434 |
Chain | Residue |
A | GLY8 |
A | ARG39 |
A | ALA40 |
A | GLY56 |
A | GLY57 |
A | TYR59 |
A | THR224 |
A | VAL226 |
A | ALA254 |
A | THR255 |
A | PRO256 |
A | GLY10 |
A | LEU366 |
A | PHE367 |
A | TRP371 |
A | GLY397 |
A | SER398 |
A | GLY406 |
A | TYR407 |
A | ILE408 |
A | ALA411 |
A | PHE11 |
A | SER12 |
A | LEU30 |
A | GLU31 |
A | GLY32 |
A | GLY37 |
A | GLY38 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GP7 A 435 |
Chain | Residue |
A | GLN99 |
A | ALA100 |
A | THR115 |
A | PHE159 |
A | LEU160 |
A | MET180 |
A | ILE191 |
A | LEU192 |
A | VAL195 |
B | ILE103 |
B | GLY105 |
B | ALA108 |
site_id | AC3 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD B 434 |
Chain | Residue |
B | VAL7 |
B | GLY8 |
B | GLY10 |
B | PHE11 |
B | SER12 |
B | LEU30 |
B | GLU31 |
B | GLY32 |
B | GLY37 |
B | GLY38 |
B | ARG39 |
B | GLY56 |
B | GLY57 |
B | TYR59 |
B | THR224 |
B | VAL225 |
B | VAL226 |
B | ALA254 |
B | THR255 |
B | PRO256 |
B | ILE263 |
B | TRP361 |
B | LEU366 |
B | PHE367 |
B | PRO370 |
B | GLY397 |
B | SER398 |
B | GLY406 |
B | TYR407 |
B | ILE408 |
B | ALA411 |
B | HOH519 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GP7 B 435 |
Chain | Residue |
A | ILE103 |
A | PRO104 |
A | GLY105 |
B | ALA100 |
B | VAL111 |
B | THR115 |
B | PHE159 |
B | LEU160 |
B | MET180 |
B | ILE191 |
B | LEU192 |
B | VAL195 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20006620, ECO:0000269|PubMed:21383134, ECO:0007744|PDB:3K7M, ECO:0007744|PDB:3K7Q, ECO:0007744|PDB:3K7T, ECO:0007744|PDB:3NG7, ECO:0007744|PDB:3NGC, ECO:0007744|PDB:3NH3, ECO:0007744|PDB:3NHO, ECO:0007744|PDB:3NK0, ECO:0007744|PDB:3NK1, ECO:0007744|PDB:3NK2, ECO:0007744|PDB:3NN0 |
Chain | Residue | Details |
A | SER12 | |
B | GLY38 | |
B | GLY56 | |
B | VAL226 | |
B | SER398 | |
B | GLY406 | |
A | GLU31 | |
A | GLY38 | |
A | GLY56 | |
A | VAL226 | |
A | SER398 | |
A | GLY406 | |
B | SER12 | |
B | GLU31 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20006620, ECO:0000269|PubMed:21383134, ECO:0007744|PDB:3K7Q, ECO:0007744|PDB:3NG7, ECO:0007744|PDB:3NGC, ECO:0007744|PDB:3NH3 |
Chain | Residue | Details |
A | ASN166 | |
A | TYR311 | |
A | PHE326 | |
A | TYR407 | |
B | ASN166 | |
B | TYR311 | |
B | PHE326 | |
B | TYR407 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20006620, ECO:0000269|PubMed:21383134, ECO:0007744|PDB:3NG7, ECO:0007744|PDB:3NGC, ECO:0007744|PDB:3NH3 |
Chain | Residue | Details |
A | TRP371 | |
B | TRP371 |