Research workbench
M. tuberculosis RV3291C complexed to lysine
Analyse M. tuberculosis RV3291C complexed to lysine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W24
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable transcriptional regulatory protein
- UniProt
- P96896
- Ligands
- LYS
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable transcriptional regulatory protein | protein | 147 | 36% helix, 30% strand | P96896 |
Ligands and binding sites
- LYS · Lysine · ligand · chains A, B
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 | 412 | 0.71 | 0.82 | 64 | empty |
| 2 | 106 | 0.65 | 0.89 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 2950 Ų buried · 57 hydrogen bonds · protein-protein
Compared structures
- 2W24 · M. tuberculosis Rv3291c complexed to Lysine · 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 P96896
- Elsewhere: RCSB PDB 2W24 · PDBe 2W24 · UniProt P96896
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