3DBM
Crystal Structure of Allene oxide synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009535 | cellular_component | chloroplast thylakoid membrane |
| A | 0009695 | biological_process | jasmonic acid biosynthetic process |
| A | 0009941 | cellular_component | chloroplast envelope |
| A | 0009978 | molecular_function | allene oxide synthase activity |
| A | 0016125 | biological_process | sterol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016829 | molecular_function | lyase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0031408 | biological_process | oxylipin biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 600 |
| Chain | Residue |
| A | LYS88 |
| A | GLY280 |
| A | LEU284 |
| A | PRO343 |
| A | GLN347 |
| A | TRP410 |
| A | ASN412 |
| A | ASN423 |
| A | LYS424 |
| A | CYS426 |
| A | ALA427 |
| A | PHE92 |
| A | GLY428 |
| A | HOH728 |
| A | HOH729 |
| A | LEU109 |
| A | HIS119 |
| A | LYS123 |
| A | LEU126 |
| A | TYR180 |
| A | ASN276 |
| A | THR277 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HO2 A 601 |
| Chain | Residue |
| A | SER199 |
| A | LEU206 |
| A | LEU212 |
| A | GLY279 |
| A | LYS282 |
| A | HOH650 |
| A | HOH670 |
| A | HOH690 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18787124","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DAM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DAN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18787124","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3DBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18787124","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DAM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DAN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
