6X0J
Structure of reduced SidA ornithine hydroxylase with the FAD "in" and complexed with NADP and L-ornithine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 24 |
| Details | binding site for residue NAP A 601 |
| Chain | Residue |
| A | LYS100 |
| A | SER257 |
| A | GLU260 |
| A | ARG279 |
| A | ASN323 |
| A | TYR324 |
| A | SER325 |
| A | ALA404 |
| A | THR405 |
| A | GLY406 |
| A | FDA603 |
| A | GLN102 |
| A | HOH701 |
| A | HOH707 |
| A | HOH743 |
| A | HOH749 |
| A | HOH764 |
| A | ARG144 |
| A | LYS215 |
| A | PRO217 |
| A | GLY253 |
| A | SER254 |
| A | GLY255 |
| A | GLN256 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ORN A 602 |
| Chain | Residue |
| A | GLN102 |
| A | ILE103 |
| A | LYS107 |
| A | ASN293 |
| A | PHE296 |
| A | ASN323 |
| A | SER469 |
| A | HOH701 |
| A | HOH718 |
| A | HOH773 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue FDA A 603 |
| Chain | Residue |
| A | GLY46 |
| A | GLY48 |
| A | PRO49 |
| A | ALA50 |
| A | LEU82 |
| A | GLU83 |
| A | ARG84 |
| A | GLN85 |
| A | TRP90 |
| A | HIS91 |
| A | MET94 |
| A | MET101 |
| A | GLN102 |
| A | ILE103 |
| A | GLU166 |
| A | GLU167 |
| A | VAL168 |
| A | ALA209 |
| A | ILE210 |
| A | GLY211 |
| A | TYR407 |
| A | ARG409 |
| A | SER466 |
| A | LEU467 |
| A | LEU468 |
| A | NAP601 |
| A | HOH717 |
| A | HOH729 |
| A | HOH761 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue NAP B 601 |
| Chain | Residue |
| B | LYS100 |
| B | GLN102 |
| B | ARG144 |
| B | PRO217 |
| B | GLY253 |
| B | SER254 |
| B | GLY255 |
| B | GLN256 |
| B | SER257 |
| B | GLU260 |
| B | ARG279 |
| B | ASN323 |
| B | TYR324 |
| B | SER325 |
| B | ALA404 |
| B | THR405 |
| B | GLY406 |
| B | ORN602 |
| B | FDA603 |
| B | HOH711 |
| B | HOH738 |
| B | HOH751 |
| B | HOH763 |
| B | HOH773 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ORN B 602 |
| Chain | Residue |
| B | GLN102 |
| B | ILE103 |
| B | LYS107 |
| B | ASN293 |
| B | PHE296 |
| B | ASN323 |
| B | SER469 |
| B | NAP601 |
| B | HOH710 |
| B | HOH714 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | binding site for residue FDA B 603 |
| Chain | Residue |
| B | PRO49 |
| B | ALA50 |
| B | LEU82 |
| B | GLU83 |
| B | ARG84 |
| B | GLN85 |
| B | TRP90 |
| B | HIS91 |
| B | MET94 |
| B | MET101 |
| B | GLN102 |
| B | ILE103 |
| B | ARG144 |
| B | GLU166 |
| B | VAL168 |
| B | ALA209 |
| B | ILE210 |
| B | GLY211 |
| B | TYR407 |
| B | SER466 |
| B | LEU467 |
| B | LEU468 |
| B | NAP601 |
| B | HOH743 |
| B | HOH744 |
| B | HOH770 |
| B | GLY46 |
| B | GLY48 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue NAP C 601 |
| Chain | Residue |
| C | LYS100 |
| C | GLN102 |
| C | ARG144 |
| C | LYS215 |
| C | PRO217 |
| C | SER254 |
| C | GLY255 |
| C | GLN256 |
| C | SER257 |
| C | GLU260 |
| C | ARG279 |
| C | ASN323 |
| C | SER325 |
| C | ALA404 |
| C | THR405 |
| C | GLY406 |
| C | TYR407 |
| C | FDA603 |
| C | HOH708 |
| C | HOH722 |
| C | HOH723 |
| C | HOH764 |
| C | HOH774 |
| C | HOH783 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue ORN C 602 |
| Chain | Residue |
| C | GLN102 |
| C | ILE103 |
| C | LYS107 |
| C | ASN293 |
| C | PHE296 |
| C | ASN323 |
| C | LEU467 |
| C | SER469 |
| C | HOH715 |
| C | HOH739 |
| C | HOH751 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | binding site for residue FDA C 603 |
| Chain | Residue |
| C | GLY46 |
| C | GLY48 |
| C | PRO49 |
| C | ALA50 |
| C | LEU82 |
| C | GLU83 |
| C | ARG84 |
| C | GLN85 |
| C | TRP90 |
| C | HIS91 |
| C | MET94 |
| C | MET101 |
| C | GLN102 |
| C | ILE103 |
| C | GLU166 |
| C | GLU167 |
| C | VAL168 |
| C | ALA209 |
| C | ILE210 |
| C | GLY211 |
| C | TYR407 |
| C | ARG409 |
| C | SER466 |
| C | LEU467 |
| C | LEU468 |
| C | NAP601 |
| C | HOH736 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for residue NAP D 601 |
| Chain | Residue |
| D | LYS100 |
| D | GLN102 |
| D | ARG144 |
| D | LYS215 |
| D | PRO217 |
| D | SER254 |
| D | GLY255 |
| D | GLN256 |
| D | SER257 |
| D | GLU260 |
| D | ARG279 |
| D | ASN323 |
| D | TYR324 |
| D | SER325 |
| D | ALA404 |
| D | THR405 |
| D | GLY406 |
| D | ORN602 |
| D | FDA603 |
| D | HOH713 |
| D | HOH729 |
| D | HOH733 |
| D | HOH743 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue ORN D 602 |
| Chain | Residue |
| D | GLN102 |
| D | ILE103 |
| D | LYS107 |
| D | ASN293 |
| D | PHE296 |
| D | ASN323 |
| D | SER469 |
| D | NAP601 |
| D | HOH719 |
| D | HOH761 |
| site_id | AD3 |
| Number of Residues | 27 |
| Details | binding site for residue FDA D 603 |
| Chain | Residue |
| D | GLY46 |
| D | GLY48 |
| D | PRO49 |
| D | ALA50 |
| D | GLU83 |
| D | ARG84 |
| D | GLN85 |
| D | TRP90 |
| D | HIS91 |
| D | MET94 |
| D | MET101 |
| D | GLN102 |
| D | ILE103 |
| D | GLU166 |
| D | GLU167 |
| D | VAL168 |
| D | ALA209 |
| D | ILE210 |
| D | GLY211 |
| D | TYR407 |
| D | ARG409 |
| D | SER466 |
| D | LEU467 |
| D | LEU468 |
| D | NAP601 |
| D | HOH726 |
| D | HOH770 |
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 |
