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The crystal structure of DHAD
Analyse The crystal structure of DHAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YM0
- Type
- protein
- Length
- 520 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.842
- Source
- Arabidopsis thaliana
- Molecule
- Dihydroxy-acid dehydratase, chloroplastic
- EC
- 4.2.1.9
- UniProt
- Q9LIR4
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.842 · 1 distinct chain · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroxy-acid dehydratase, chloroplastic (EC 4.2.1.9) | protein | 520 | 41% helix, 13% strand | Q9LIR4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.69 | 0.80 | 54 | SO4 |
| 2 | 52 | 0.37 | 0.80 | 10 | empty |
| 3 | 52 | 0.29 | 0.75 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9LIR4
- Elsewhere: RCSB PDB 5YM0 · PDBe 5YM0 · UniProt Q9LIR4
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