Research workbench
Structure of L-2-keto-3-deoxyarabonate dehydratase
Analyse Structure of L-2-keto-3-deoxyarabonate dehydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FKK
- Type
- protein
- Length
- 608 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-2-keto-3-deoxyarabonate dehydratase
- UniProt
- Q1JUQ0
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-2-keto-3-deoxyarabonate dehydratase | protein | 304 | 53% helix, 12% strand | Q1JUQ0 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.85 | 0.93 | 44 | empty |
| 2 | 311 | 0.63 | 0.79 | 38 | empty |
| 3 | 313 | 0.63 | 0.79 | 35 | empty |
| 4 | 101 | 0.42 | 0.78 | 19 | empty |
| 5 | 69 | 0.40 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1591 Ų buried · 16 hydrogen bonds · protein-protein
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 Q1JUQ0
- Elsewhere: RCSB PDB 3FKK · PDBe 3FKK · UniProt Q1JUQ0
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