6X0H
Structure of oxidized SidA ornithine hydroxylase with the FAD in the "out" conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0010106 | biological_process | cellular response to iron ion starvation |
| A | 0019290 | biological_process | siderophore biosynthetic process |
| A | 0031169 | biological_process | ferrichrome biosynthetic process |
| A | 0031172 | molecular_function | ornithine N5-monooxygenase activity |
| A | 0033214 | biological_process | siderophore-iron import into cell |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006696 | biological_process | ergosterol biosynthetic process |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0010106 | biological_process | cellular response to iron ion starvation |
| B | 0019290 | biological_process | siderophore biosynthetic process |
| B | 0031169 | biological_process | ferrichrome biosynthetic process |
| B | 0031172 | molecular_function | ornithine N5-monooxygenase activity |
| B | 0033214 | biological_process | siderophore-iron import into cell |
| B | 0044550 | biological_process | secondary metabolite biosynthetic process |
| B | 0070401 | molecular_function | NADP+ binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006696 | biological_process | ergosterol biosynthetic process |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0010106 | biological_process | cellular response to iron ion starvation |
| C | 0019290 | biological_process | siderophore biosynthetic process |
| C | 0031169 | biological_process | ferrichrome biosynthetic process |
| C | 0031172 | molecular_function | ornithine N5-monooxygenase activity |
| C | 0033214 | biological_process | siderophore-iron import into cell |
| C | 0044550 | biological_process | secondary metabolite biosynthetic process |
| C | 0070401 | molecular_function | NADP+ binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0006696 | biological_process | ergosterol biosynthetic process |
| D | 0006879 | biological_process | intracellular iron ion homeostasis |
| D | 0010106 | biological_process | cellular response to iron ion starvation |
| D | 0019290 | biological_process | siderophore biosynthetic process |
| D | 0031169 | biological_process | ferrichrome biosynthetic process |
| D | 0031172 | molecular_function | ornithine N5-monooxygenase activity |
| D | 0033214 | biological_process | siderophore-iron import into cell |
| D | 0044550 | biological_process | secondary metabolite biosynthetic process |
| D | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | GLY46 |
| A | HIS91 |
| A | MET94 |
| A | ARG144 |
| A | GLU166 |
| A | GLU167 |
| A | VAL168 |
| A | ALA209 |
| A | ILE210 |
| A | GLY211 |
| A | TYR324 |
| A | GLY48 |
| A | TYR407 |
| A | ARG409 |
| A | SER466 |
| A | LEU467 |
| A | LEU468 |
| A | HOH747 |
| A | HOH767 |
| A | HOH784 |
| A | HOH796 |
| A | HOH808 |
| A | PRO49 |
| A | ALA50 |
| A | LEU82 |
| A | GLU83 |
| A | ARG84 |
| A | GLN85 |
| A | TRP90 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 602 |
| Chain | Residue |
| A | ILE103 |
| A | LYS107 |
| A | PHE296 |
| A | SER469 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PGE A 603 |
| Chain | Residue |
| A | ARG84 |
| A | SER92 |
| A | LYS231 |
| A | HOH803 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CA A 604 |
| Chain | Residue |
| A | SER138 |
| B | ASP288 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 601 |
| Chain | Residue |
| B | GLY46 |
| B | GLY48 |
| B | PRO49 |
| B | ALA50 |
| B | LEU82 |
| B | GLU83 |
| B | ARG84 |
| B | GLN85 |
| B | TRP90 |
| B | HIS91 |
| B | MET94 |
| B | GLU166 |
| B | GLU167 |
| B | VAL168 |
| B | ALA209 |
| B | ILE210 |
| B | GLY211 |
| B | ASN323 |
| B | TYR324 |
| B | TYR407 |
| B | ARG409 |
| B | SER466 |
| B | LEU467 |
| B | LEU468 |
| B | HOH710 |
| B | HOH757 |
| B | HOH772 |
| B | HOH784 |
| B | HOH785 |
| B | HOH790 |
| B | HOH832 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 602 |
| Chain | Residue |
| B | ILE103 |
| B | LYS107 |
| B | PHE296 |
| B | SER469 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue FAD C 601 |
| Chain | Residue |
| C | HOH795 |
| C | HOH801 |
| C | GLY46 |
| C | GLY48 |
| C | PRO49 |
| C | ALA50 |
| C | GLU83 |
| C | ARG84 |
| C | GLN85 |
| C | TRP90 |
| C | HIS91 |
| C | MET94 |
| C | GLU166 |
| C | GLU167 |
| C | VAL168 |
| C | ALA209 |
| C | ILE210 |
| C | GLY211 |
| C | TYR324 |
| C | TYR407 |
| C | ARG409 |
| C | SER466 |
| C | LEU468 |
| C | HOH703 |
| C | HOH728 |
| C | HOH746 |
| C | HOH774 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT C 602 |
| Chain | Residue |
| C | ILE103 |
| C | LYS107 |
| C | PHE296 |
| C | SER469 |
| C | HOH784 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CA C 603 |
| Chain | Residue |
| C | SER138 |
| C | HOH811 |
| D | ASP288 |
| site_id | AD1 |
| Number of Residues | 25 |
| Details | binding site for residue FAD D 601 |
| Chain | Residue |
| D | GLY46 |
| D | GLY48 |
| D | PRO49 |
| D | ALA50 |
| D | LEU82 |
| D | GLU83 |
| D | ARG84 |
| D | GLN85 |
| D | TRP90 |
| D | HIS91 |
| D | MET94 |
| D | ARG144 |
| D | GLU166 |
| D | VAL168 |
| D | ALA209 |
| D | ILE210 |
| D | GLY211 |
| D | TYR324 |
| D | TYR407 |
| D | ARG409 |
| D | SER466 |
| D | LEU468 |
| D | HOH722 |
| D | HOH737 |
| D | HOH745 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT D 602 |
| Chain | Residue |
| D | ILE103 |
| D | LYS107 |
| D | PHE296 |
| D | SER469 |
| D | HOH775 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22928747","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






