Research workbench
Crystal structure of an acetolactate decarboxylase from klebsiella pneumoniae
Analyse Crystal structure of an acetolactate decarboxylase from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6INB
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-acetolactate decarboxylase
- EC
- 4.1.1.5
- UniProt
- W9BHF3
- Ligands
- ZN, CL
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-acetolactate decarboxylase (EC 4.1.1.5) | protein | 219 | 17% helix, 47% strand | W9BHF3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.56 | 0.78 | 22 | empty |
Compared structures
- 6INB · Crystal structure of an acetolactate decarboxylase from Klebsiella pneumoniae · 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 W9BHF3
- Elsewhere: RCSB PDB 6INB · PDBe 6INB · UniProt W9BHF3
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