MolNFT v2 · #129950 · protein
Catabolism of the Cholesterol Side Chain in Mycobacterium tuberculosis is Controlled by a Redox-Sensitive Thiol Switch
5ONC: “Catabolism of the Cholesterol Side Chain in Mycobacterium tuberculosis is Controlled by a Redox-Sensitive…”. X-ray diffraction at 2.19, 1 ligand (CL). MolNFT v2 #129950 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ONC
- Type
- protein
- Length
- 725 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.19
- Source
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- UniProt
- I6XHI4
- Ligands
- CL
Structure
x-ray diffraction · resolution 2.19 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 366 | — | I6XHI4 |
| B | — | protein | 359 | — | I6XHI4 |
Ligands and binding sites
- CL · Chloride ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ONC · Catabolism of the cholesterol side chain in mycobacterium tuberculosis is controlled by a… · the same entry in another collection · chain A against A, TM-score 1.00
- I6XHI4 · AlphaFold monomer V2.0 prediction for steroid 3-ketoacyl-CoA thiolase (I6XHI4) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 I6XHI4
- Elsewhere: RCSB PDB 5ONC · PDBe 5ONC · UniProt I6XHI4
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