4KVK
Crystal structure of Oryza sativa fatty acid alpha-dioxygenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001561 | biological_process | fatty acid alpha-oxidation |
A | 0004601 | molecular_function | peroxidase activity |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0006952 | biological_process | defense response |
A | 0006979 | biological_process | response to oxidative stress |
A | 0009627 | biological_process | systemic acquired resistance |
A | 0009737 | biological_process | response to abscisic acid |
A | 0009751 | biological_process | response to salicylic acid |
A | 0012511 | cellular_component | monolayer-surrounded lipid storage body |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
A | 0020037 | molecular_function | heme binding |
A | 0031408 | biological_process | oxylipin biosynthetic process |
A | 0034614 | biological_process | cellular response to reactive oxygen species |
A | 0042742 | biological_process | defense response to bacterium |
A | 0046872 | molecular_function | metal ion binding |
A | 0050832 | biological_process | defense response to fungus |
A | 0051213 | molecular_function | dioxygenase activity |
A | 0071446 | biological_process | cellular response to salicylic acid stimulus |
A | 0071732 | biological_process | cellular response to nitric oxide |
A | 0098869 | biological_process | cellular oxidant detoxification |
A | 1902609 | biological_process | (R)-2-hydroxy-alpha-linolenic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 701 |
Chain | Residue |
A | ALA149 |
A | THR376 |
A | TYR379 |
A | MET381 |
A | HIS382 |
A | ILE416 |
A | PHE453 |
A | LEU472 |
A | LEU475 |
A | ARG479 |
A | ARG483 |
A | ILE152 |
A | HOH815 |
A | HOH843 |
A | HOH996 |
A | HOH1180 |
A | GLN153 |
A | VAL156 |
A | HIS157 |
A | ASP161 |
A | HIS162 |
A | ASN260 |
A | TRP262 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE DMU A 702 |
Chain | Residue |
A | SER19 |
A | LYS20 |
A | MET21 |
A | SER22 |
A | PHE23 |
A | LYS26 |
A | PHE31 |
A | ARG38 |
A | ILE348 |
A | PG4709 |
A | HOH829 |
A | HOH928 |
A | HOH1055 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PG4 A 703 |
Chain | Residue |
A | ASN54 |
A | ARG57 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG A 704 |
Chain | Residue |
A | PHE24 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 1PE A 705 |
Chain | Residue |
A | ASN39 |
A | HIS42 |
A | LYS43 |
A | ARG492 |
A | ILE498 |
A | PRO499 |
A | ILE500 |
A | ASP505 |
A | GLU536 |
A | NA717 |
A | HOH832 |
A | HOH1029 |
A | HOH1117 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGE A 706 |
Chain | Residue |
A | GLU490 |
A | ARG493 |
A | ARG494 |
A | PHE496 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 A 707 |
Chain | Residue |
A | ARG590 |
A | LYS606 |
A | SER608 |
A | TYR618 |
A | NA718 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 708 |
Chain | Residue |
A | ILE239 |
A | GLY240 |
A | ASP241 |
A | GLY243 |
A | LYS274 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 A 709 |
Chain | Residue |
A | ALA34 |
A | PHE35 |
A | ARG38 |
A | DMU702 |
A | HOH1119 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 710 |
Chain | Residue |
A | LYS323 |
A | ARG326 |
A | HOH1023 |
A | HOH1028 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 711 |
Chain | Residue |
A | ARG517 |
A | ALA518 |
A | ILE519 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 712 |
Chain | Residue |
A | THR210 |
A | TRP212 |
A | ASP214 |
A | SER216 |
A | HOH874 |
A | HOH1085 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 713 |
Chain | Residue |
A | LYS309 |
A | TRP333 |
A | HOH1132 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 714 |
Chain | Residue |
A | ARG330 |
A | LYS339 |
A | HOH954 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 715 |
Chain | Residue |
A | GLY350 |
A | ILE352 |
A | LEU353 |
A | HOH922 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 716 |
Chain | Residue |
A | HIS311 |
A | TYR379 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 717 |
Chain | Residue |
A | HOH981 |
A | HOH1117 |
A | ASP505 |
A | 1PE705 |
A | HOH980 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 718 |
Chain | Residue |
A | SER608 |
A | PG4707 |
A | HOH1228 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298 |
Chain | Residue | Details |
A | HIS157 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23934749 |
Chain | Residue | Details |
A | ASP158 | |
A | GLU599 | |
A | HIS162 | |
A | THR210 | |
A | TRP212 | |
A | ASP214 | |
A | SER216 | |
A | HIS311 | |
A | ARG479 | |
A | ARG483 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:23934749 |
Chain | Residue | Details |
A | HIS382 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00298 |
Chain | Residue | Details |
A | ARG259 |