Research workbench
X-ray crystal structure of alpha-acetolactate decarboxylase from bacillus subtilis strain 168
Analyse X-ray crystal structure of alpha-acetolactate decarboxylase from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XNE
- Type
- protein
- Length
- 469 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-acetolactate decarboxylase
- EC
- 4.1.1.5
- UniProt
- Q04777
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Alpha-acetolactate decarboxylase (EC 4.1.1.5) | protein | 234 | 21% helix, 45% strand | Q04777 |
| A | Alpha-acetolactate decarboxylase (EC 4.1.1.5) | protein | 235 | 20% helix, 45% strand | Q04777 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.58 | 0.77 | 51 | empty |
| 2 | 209 | 0.51 | 0.77 | 33 | empty |
| 3 | 52 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- B–A · 1203 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5XNE · X-ray Crystal Structure of alpha-acetolactate decarboxylase from Bacillus subtilis strain… · the same entry in another collection · chain B against B, TM-score 1.00
- Q04777 · AlphaFold monomer V2.0 prediction for alpha-acetolactate decarboxylase (Q04777) · a predicted model of the same protein · chain B 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 Q04777
- Elsewhere: RCSB PDB 5XNE · PDBe 5XNE · UniProt Q04777
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