Research workbench
SER480ALA mutant of L-arabinonate dehydratase
Analyse SER480ALA mutant of L-arabinonate dehydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J85
- Type
- protein
- Length
- 576 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroxyacid DEHYDRATASE/PHOSPHOGLUCONATE dehydratase
- UniProt
- I9XDU6
- Ligands
- FES, MG
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroxyacid DEHYDRATASE/PHOSPHOGLUCONATE dehydratase | protein | 576 | 38% helix, 14% strand | I9XDU6 |
Ligands and binding sites
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 | 419 | 0.57 | 0.74 | 50 | FES |
| 2 | 68 | 0.31 | 0.74 | 15 | empty |
| 3 | 60 | 0.28 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 5J85 · Ser480Ala mutant of L-arabinonate dehydratase · 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 I9XDU6
- Elsewhere: RCSB PDB 5J85 · PDBe 5J85 · UniProt I9XDU6
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