Research workbench
The structure of acc oxidase
Analyse The structure of acc oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WA6
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-aminocyclopropane-1-carboxylate oxidase 1
- EC
- 1.14.17.4
- UniProt
- Q08506
- Ligands
- FE2, PO4, SO4
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | 1-aminocyclopropane-1-carboxylate oxidase 1 (EC 1.14.17.4) | protein | 298 | 41% helix, 20% strand | Q08506 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains X
- PO4 · Phosphate ion · ion · 2 copies · chains X
- SO4 · Sulfate ion · ion · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.60 | 0.77 | 45 | FE2, PO4 |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
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 Q08506
- Elsewhere: RCSB PDB 1WA6 · PDBe 1WA6 · UniProt Q08506
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.