Research workbench
Crystal structure of the response regulator protein prra complexed with MG2+
Analyse Crystal structure of the response regulator protein prra complexed with MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YS7
- Type
- protein
- Length
- 450 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein prra
- UniProt
- Q10531
- Ligands
- MG
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulatory protein prra | protein | 224 | 38% helix, 21% strand | Q10531 |
| B | Transcriptional regulatory protein prra | protein | 226 | 40% helix, 22% strand | Q10531 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains B, A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.74 | 0.77 | 79 | TRS |
| 2 | 82 | 0.33 | 0.75 | 15 | MG |
| 3 | 60 | 0.28 | 0.74 | 15 | GOL |
Interfaces
1 interface between chains.
- A–B · 506 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1YS7 · Crystal structure of the response regulator protein prrA complexed with Mg2+ · 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 Q10531
- Elsewhere: RCSB PDB 1YS7 · PDBe 1YS7 · UniProt Q10531
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