Research workbench
RV2466C mediates the activation of TP053 to kill replicating and non- replicating mycobacterium tuberculosis
Analyse RV2466C mediates the activation of TP053 to kill replicating and non… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NXI
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- O53193
- Ligands
- MG
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 193 | 52% helix, 17% strand | O53193 |
| B | Uncharacterized protein | protein | 198 | 53% helix, 16% strand | O53193 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 5 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.46 | 0.77 | 34 | empty |
| 2 | 104 | 0.38 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2261 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 4NXI · Rv2466c Mediates the Activation of TP053 To Kill Replicating and Non-replicating… · the same entry in another collection · chain A against A, TM-score 1.00
- O53193 · AlphaFold monomer V2.0 prediction for thioredoxin-like reductase RV2466C (O53193) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 O53193
- Elsewhere: RCSB PDB 4NXI · PDBe 4NXI · UniProt O53193
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