Research workbench
Structure of a lipoate-protein ligase B from mycobacterium tuberculosis
Analyse Structure of a lipoate-protein ligase B from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W66
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoyltransferase
- EC
- 2.3.1.-
- UniProt
- Q10404
- Ligands
- DKA
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoyltransferase (EC 2.3.1.-) | protein | 218 | 30% helix, 29% strand | Q10404 |
Ligands and binding sites
- DKA · Decanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.54 | 0.82 | 35 | DKA |
| 2 | 56 | 0.51 | 0.87 | 25 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1W66 · Structure of a lipoate-protein ligase b from Mycobacterium tuberculosis · 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 Q10404
- Elsewhere: RCSB PDB 1W66 · PDBe 1W66 · UniProt Q10404
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