Research workbench
Crystal structure of probable transcriptional regulatory protein RHA5900
Analyse Crystal structure of probable transcriptional regulatory protein RHA5900 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IBD
- Type
- protein
- Length
- 380 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible transcriptional regulator
- UniProt
- Q0S7V2
- Ligands
- MG
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible transcriptional regulator | protein | 192 | 74% helix, 1% strand | Q0S7V2 |
| B | Possible transcriptional regulator | protein | 188 | 73% helix, 1% strand | Q0S7V2 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 764 | 0.76 | 0.80 | 71 | MG |
| 2 | 61 | 0.74 | 0.98 | 20 | empty |
| 3 | 54 | 0.26 | 0.73 | 13 | empty |
| 4 | 51 | 0.24 | 0.72 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1878 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2IBD · Crystal structure of Probable transcriptional regulatory protein RHA5900 · the same entry in another collection · chain A against A, TM-score 1.00
- Q0S7V2 · AlphaFold monomer V2.0 prediction for hth-type transcriptional repressor KSTR2 (Q0S7V2) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q0S7V2
- Elsewhere: RCSB PDB 2IBD · PDBe 2IBD · UniProt Q0S7V2
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