Research workbench
Edds lyase variant D290M/Y320M with bound fumarate
Analyse Edds lyase variant D290M/Y320M with bound fumarate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RX8
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Argininosuccinate lyase
- UniProt
- Q11KV9
- Ligands
- FUM, NA
- Pockets
- 6 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Argininosuccinate lyase | protein | 497 | 69% helix, 4% strand | Q11KV9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.49 | 0.78 | 20 | empty |
| 2 | 71 | 0.39 | 0.78 | 17 | empty |
| 3 | 75 | 0.37 | 0.77 | 17 | empty |
| 4 | 75 | 0.33 | 0.75 | 15 | empty |
| 5 | 64 | 0.31 | 0.75 | 17 | empty |
Compared structures
- 6RX8 · EDDS lyase variant D290M/Y320M with bound fumarate · the same entry in another collection · 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 Q11KV9
- Elsewhere: RCSB PDB 6RX8 · PDBe 6RX8 · UniProt Q11KV9
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