Research workbench
Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate
Analyse Structure of arabidopsis fatty acid amide hydrolase in complex with methyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DII
- Type
- protein
- Length
- 7,275 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid amide hydrolase
- EC
- 3.5.1.99
- UniProt
- Q7XJJ7
- Ligands
- GJY
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Fatty acid amide hydrolase (EC 3.5.1.99) | protein | 602 | 41% helix, 14% strand | Q7XJJ7 |
| B, D, F | Fatty acid amide hydrolase (EC 3.5.1.99) | protein | 605 | 40% helix, 13% strand | Q7XJJ7 |
| H, J, L | Fatty acid amide hydrolase (EC 3.5.1.99) | protein | 616 | 39% helix, 14% strand | Q7XJJ7 |
Ligands and binding sites
- GJY · methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1119 | 0.87 | 0.88 | 143 | GJY |
| 2 | 1035 | 0.87 | 0.88 | 130 | GJY |
| 3 | 992 | 0.87 | 0.88 | 133 | GJY |
| 4 | 687 | 0.85 | 0.89 | 96 | GJY |
| 5 | 771 | 0.84 | 0.88 | 108 | GJY |
Interfaces
14 interfaces between chains.
- K–L · 1831 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1820 Ų buried · 20 hydrogen bonds · protein-protein
- I–J · 1783 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1731 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1728 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 covalent (covalent ligand).
Compared structures
- 6DII · Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl… · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q7XJJ7
- Elsewhere: RCSB PDB 6DII · PDBe 6DII · UniProt Q7XJJ7
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