4KVK
Crystal structure of Oryza sativa fatty acid alpha-dioxygenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001676 | biological_process | long-chain fatty acid metabolic process |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 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 | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0102672 | molecular_function | fatty acid alpha-dioxygenase activity |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23934749","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23934749","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
