3DY5
Allene oxide synthase 8R-lipoxygenase from Plexaura homomalla
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| 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 | 0016829 | molecular_function | lyase activity |
| A | 0019369 | biological_process | arachidonate metabolic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0031408 | biological_process | oxylipin biosynthetic process |
| A | 0034440 | biological_process | lipid oxidation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047677 | molecular_function | arachidonate 8(R)-lipoxygenase activity |
| A | 0051213 | molecular_function | dioxygenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019369 | biological_process | arachidonate metabolic process |
| C | 0020037 | molecular_function | heme binding |
| C | 0031408 | biological_process | oxylipin biosynthetic process |
| C | 0034440 | biological_process | lipid oxidation |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047677 | molecular_function | arachidonate 8(R)-lipoxygenase activity |
| C | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A1099 |
| Chain | Residue |
| A | HIS757 |
| A | HIS762 |
| A | HIS943 |
| A | ASN947 |
| A | ILE1066 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C1099 |
| Chain | Residue |
| C | ILE1066 |
| C | HIS757 |
| C | HIS762 |
| C | HIS943 |
| C | ASN947 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A1100 |
| Chain | Residue |
| A | PHE53 |
| A | ARG64 |
| A | ALA65 |
| A | THR66 |
| A | HIS67 |
| A | ARG102 |
| A | SER118 |
| A | SER120 |
| A | VAL135 |
| A | MET136 |
| A | ASN137 |
| A | SER194 |
| A | GLN195 |
| A | PHE322 |
| A | ARG349 |
| A | VAL352 |
| A | TYR353 |
| A | GLN357 |
| A | ARG360 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM C1100 |
| Chain | Residue |
| C | PHE53 |
| C | ARG64 |
| C | ALA65 |
| C | THR66 |
| C | HIS67 |
| C | ARG102 |
| C | SER118 |
| C | SER120 |
| C | VAL135 |
| C | MET136 |
| C | ASN137 |
| C | SER194 |
| C | GLN195 |
| C | PHE322 |
| C | ARG349 |
| C | VAL352 |
| C | TYR353 |
| C | GLN357 |
| C | ARG360 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16162493","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lnh |
| Chain | Residue | Details |
| A | ASN947 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lnh |
| Chain | Residue | Details |
| C | ASN947 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lnh |
| Chain | Residue | Details |
| A | TYR193 | |
| A | ASN137 | |
| A | THR66 | |
| A | HIS67 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lnh |
| Chain | Residue | Details |
| C | TYR193 | |
| C | ASN137 | |
| C | THR66 | |
| C | HIS67 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 758 |
| Chain | Residue | Details |
| A | THR66 | electrostatic stabiliser |
| A | HIS67 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASN137 | electrostatic stabiliser |
| A | TYR353 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 758 |
| Chain | Residue | Details |
