4B68
A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Arg
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 | 14 |
Details | BINDING SITE FOR RESIDUE ARG A 503 |
Chain | Residue |
A | GLN102 |
A | NAP1493 |
A | HOH2047 |
A | HOH2050 |
A | HOH2134 |
A | HOH2153 |
A | ILE103 |
A | LYS107 |
A | ASN293 |
A | PHE296 |
A | THR322 |
A | ASN323 |
A | LEU467 |
A | SER469 |
site_id | AC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 1492 |
Chain | Residue |
A | GLY46 |
A | GLY48 |
A | PRO49 |
A | ALA50 |
A | LEU82 |
A | GLU83 |
A | ARG84 |
A | GLN85 |
A | TRP90 |
A | HIS91 |
A | MET101 |
A | GLN102 |
A | ILE103 |
A | ARG144 |
A | GLU166 |
A | GLU167 |
A | VAL168 |
A | ILE210 |
A | GLY211 |
A | TYR407 |
A | SER466 |
A | LEU467 |
A | LEU468 |
A | NAP1493 |
A | GOL1500 |
A | HOH2015 |
A | HOH2028 |
A | HOH2029 |
A | HOH2108 |
A | HOH2229 |
A | HOH2236 |
site_id | AC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAP A 1493 |
Chain | Residue |
A | LYS100 |
A | GLN102 |
A | ARG144 |
A | PRO217 |
A | SER254 |
A | GLY255 |
A | GLN256 |
A | SER257 |
A | GLU260 |
A | ARG279 |
A | ASN323 |
A | SER325 |
A | ALA404 |
A | THR405 |
A | GLY406 |
A | TYR407 |
A | ARG503 |
A | FAD1492 |
A | GOL1500 |
A | HOH2125 |
A | HOH2132 |
A | HOH2133 |
A | HOH2142 |
A | HOH2144 |
A | HOH2179 |
A | HOH2202 |
A | HOH2243 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1494 |
Chain | Residue |
A | LEU125 |
A | HIS126 |
A | GLY129 |
A | ARG130 |
A | LEU131 |
A | ILE132 |
A | HOH2244 |
A | HOH2245 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1495 |
Chain | Residue |
A | CYS80 |
A | SER159 |
A | ASP160 |
A | VAL162 |
A | ARG201 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1496 |
Chain | Residue |
A | HIS133 |
A | GLU294 |
A | TYR336 |
A | MET339 |
A | TYR340 |
A | ARG343 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1497 |
Chain | Residue |
A | GLN420 |
A | ARG423 |
A | GLY426 |
A | GLN427 |
A | ASP428 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1498 |
Chain | Residue |
A | ASN337 |
A | LEU341 |
A | HOH2043 |
A | PRO142 |
A | ALA143 |
A | GLU146 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1499 |
Chain | Residue |
A | LYS128 |
A | ASP149 |
A | ARG152 |
A | GLN156 |
A | PRO178 |
A | HOH2088 |
A | HOH2247 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1500 |
Chain | Residue |
A | ARG409 |
A | FAD1492 |
A | NAP1493 |
A | HOH2176 |
A | HOH2204 |
A | HOH2229 |
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 | ASN323 | |
A | SER466 |