5CKU
Structure of Aspergillus fumigatus ornithine hydroxylase (SidA) mutant N323A bound to NADP and 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 | 0005575 | cellular_component | cellular_component |
| 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-dependent iron import into cell |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| A | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | GLY46 |
| A | HIS91 |
| A | MET94 |
| A | MET101 |
| A | GLN102 |
| A | ILE103 |
| A | GLU166 |
| A | GLU167 |
| A | VAL168 |
| A | ALA209 |
| A | ILE210 |
| A | GLY48 |
| A | GLY211 |
| A | TYR407 |
| A | ARG409 |
| A | SER466 |
| A | LEU467 |
| A | LEU468 |
| A | HOH715 |
| A | HOH769 |
| A | HOH789 |
| A | HOH791 |
| A | PRO49 |
| A | HOH820 |
| A | HOH829 |
| A | ALA50 |
| A | LEU82 |
| A | GLU83 |
| A | ARG84 |
| A | GLN85 |
| A | TRP90 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue NAP A 602 |
| Chain | Residue |
| A | PRO217 |
| A | SER254 |
| A | GLY255 |
| A | GLN256 |
| A | SER257 |
| A | ARG279 |
| A | TYR324 |
| A | SER325 |
| A | ALA404 |
| A | THR405 |
| A | GLY406 |
| A | HOH713 |
| A | HOH760 |
| A | HOH778 |
| A | HOH793 |
| A | HOH838 |
| A | HOH857 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue ORN A 603 |
| Chain | Residue |
| A | ILE103 |
| A | LYS107 |
| A | ASN293 |
| A | PHE296 |
| A | LEU467 |
| A | SER469 |
| A | HOH708 |
| A | HOH794 |
| A | HOH815 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | ARG364 |
| A | GLU366 |
| A | HIS367 |
| A | HIS368 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | HIS421 |
| A | LYS444 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | LEU125 |
| A | HIS126 |
| A | GLY129 |
| A | ARG130 |
| A | LEU131 |
| A | ILE132 |
| A | HOH822 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 607 |
| Chain | Residue |
| A | PHE291 |
| A | GLU294 |
| A | TYR336 |
| A | MET339 |
| A | TYR340 |
| A | ARG343 |
| A | TRP352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22928747 |
| Chain | Residue | Details |
| A | GLU83 | |
| A | SER469 | |
| A | GLN102 | |
| A | LYS107 | |
| A | VAL168 | |
| A | SER254 | |
| A | ARG279 | |
| A | ASN293 | |
| A | ALA323 | |
| A | SER466 |
