Research workbench
X-ray structure of allene oxide cyclase from arabidopsis thaliana AT3G25770
Analyse X-ray structure of allene oxide cyclase from arabidopsis thaliana AT3G25770 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z8K
- Type
- protein
- Length
- 522 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AT3G25770 protein
- EC
- 5.3.99.6
- UniProt
- Q9LS02
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | AT3G25770 protein (EC 5.3.99.6) | protein | 174 | 9% helix, 48% strand | Q9LS02 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.70 | 0.90 | 20 | empty |
| 2 | 104 | 0.70 | 0.91 | 20 | empty |
| 3 | 128 | 0.68 | 0.89 | 21 | empty |
| 4 | 104 | 0.55 | 0.85 | 29 | empty |
| 5 | 225 | 0.52 | 0.76 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–C · 959 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 953 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 925 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1Z8K · X-ray structure of allene oxide cyclase from Arabidopsis thaliana at3g25770 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LS02 · AlphaFold monomer V2.0 prediction for allene oxide cyclase 2, chloroplastic (Q9LS02) · a predicted model of the same protein · chain A against A, 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 Q9LS02
- Elsewhere: RCSB PDB 1Z8K · PDBe 1Z8K · UniProt Q9LS02
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