MolNFT v1 · #135775 · protein
Structure of the regulatory domain of the arac family transcriptional activator rhar
5U93 · Hth-type transcriptional activator rhar: “Structure of the regulatory domain of the arac family transcriptional activator rhar”. X-ray diffraction, 2 ligands (RM4, NI), 3 pockets (best druggability 0.49). MolNFT v1 #135775 on…
- PDB
- 5U93
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional activator rhar
- UniProt
- C5A074
- Ligands
- RM4, NI
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional activator rhar | protein | 160 | 29% helix, 36% strand | C5A074 |
| B | Hth-type transcriptional activator rhar | protein | 161 | 30% helix, 37% strand | C5A074 |
Ligands and binding sites
- RM4 · beta-L-rhamnopyranose · ligand · 2 copies · chains A, B
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.49 | 0.79 | 25 | empty |
| 2 | 79 | 0.40 | 0.78 | 22 | empty |
| 3 | 50 | 0.35 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 937 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 5U93 · Structure of the Regulatory Domain of the AraC Family Transcriptional Activator RhaR · the same entry in another collection · chain A against A, TM-score 1.00
- C5A074 · AlphaFold monomer V2.0 prediction for hth-type transcriptional activator rhar (C5A074) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 C5A074
- Elsewhere: RCSB PDB 5U93 · PDBe 5U93 · UniProt C5A074
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