4KVJ
Crystal structure of Oryza sativa fatty acid alpha-dioxygenase with hydrogen peroxide
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 | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 701 |
| Chain | Residue |
| A | ALA149 |
| A | ARG380 |
| A | HIS382 |
| A | ILE416 |
| A | PHE453 |
| A | LEU472 |
| A | LEU475 |
| A | ARG479 |
| A | ARG483 |
| A | PEO719 |
| A | HOH843 |
| A | ILE152 |
| A | HOH932 |
| A | HOH1048 |
| A | GLN153 |
| A | ASP161 |
| A | HIS162 |
| A | ASN260 |
| A | TRP262 |
| A | THR376 |
| A | TYR379 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DMU A 702 |
| Chain | Residue |
| A | SER19 |
| A | LYS20 |
| A | MET21 |
| A | SER22 |
| A | PHE23 |
| A | PHE24 |
| A | LYS26 |
| A | PHE31 |
| A | ARG38 |
| A | LEU51 |
| A | ILE348 |
| A | LEU353 |
| A | PEG704 |
| A | PEG709 |
| A | HOH813 |
| A | HOH973 |
| A | HOH1102 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 703 |
| Chain | Residue |
| A | PRO47 |
| A | LEU50 |
| A | ARG57 |
| A | ALA328 |
| A | ILE352 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 704 |
| Chain | Residue |
| A | GLY28 |
| A | DMU702 |
| A | PEG712 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE P33 A 705 |
| Chain | Residue |
| A | LYS37 |
| A | ASN39 |
| A | LYS43 |
| A | ARG492 |
| A | ILE498 |
| A | PRO499 |
| A | ASP505 |
| A | GLU546 |
| A | NA720 |
| A | HOH848 |
| A | HOH969 |
| A | HOH1082 |
| A | HOH1083 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 706 |
| Chain | Residue |
| A | GLU490 |
| A | ARG493 |
| A | ARG494 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 707 |
| Chain | Residue |
| A | ARG590 |
| A | LYS606 |
| A | SER608 |
| A | NA721 |
| A | HOH1004 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 708 |
| Chain | Residue |
| A | ILE239 |
| A | GLY240 |
| A | GLY243 |
| A | LYS274 |
| A | ASN455 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 709 |
| Chain | Residue |
| A | PHE345 |
| A | DMU702 |
| A | HOH1081 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 710 |
| Chain | Residue |
| A | LYS323 |
| A | ARG326 |
| A | HOH871 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 712 |
| Chain | Residue |
| A | PEG704 |
| A | HOH1087 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 713 |
| Chain | Residue |
| A | HIS42 |
| A | LYS43 |
| A | ARG330 |
| A | HOH852 |
| A | HOH1091 |
| A | HOH1106 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 714 |
| Chain | Residue |
| A | ASP158 |
| A | THR210 |
| A | TRP212 |
| A | ASP214 |
| A | SER216 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 715 |
| Chain | Residue |
| A | LYS309 |
| A | TRP333 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 716 |
| Chain | Residue |
| A | ARG330 |
| A | LYS339 |
| A | HOH896 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 717 |
| Chain | Residue |
| A | HOH1013 |
| A | GLY350 |
| A | ILE352 |
| A | LEU353 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 718 |
| Chain | Residue |
| A | HIS311 |
| A | TYR379 |
| A | ARG559 |
| A | HOH886 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEO A 719 |
| Chain | Residue |
| A | GLN153 |
| A | HIS157 |
| A | ASN260 |
| A | HEM701 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 720 |
| Chain | Residue |
| A | ASP505 |
| A | P33705 |
| A | HOH969 |
| A | HOH1083 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 721 |
| Chain | Residue |
| A | SER608 |
| A | PG4707 |
| A | HOH1004 |
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 |
