Research workbench
Pyrr, the bacillus subtilis pyrimidine biosynthetic operon repressor, hexameric form
Analyse Pyrr, the bacillus subtilis pyrimidine biosynthetic operon repressor, hexameric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A4X
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyrimidine operon regulatory protein pyrr
- UniProt
- P39765
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrimidine operon regulatory protein pyrr | protein | 167 | 31% helix, 33% strand | P39765 |
| B | Pyrimidine operon regulatory protein pyrr | protein | 167 | 31% helix, 33% strand | P39765 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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 | 136 | 0.49 | 0.79 | 30 | SO4 |
| 2 | 120 | 0.43 | 0.76 | 23 | SO4 |
| 3 | 69 | 0.31 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 818 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1A4X · Pyrr, the bacillus subtilis pyrimidine biosynthetic operon repressor, hexameric form · the same entry in another collection · chain A against A, TM-score 1.00
- P39765 · AlphaFold monomer V2.0 prediction for bifunctional protein pyrr (P39765) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P39765
- Elsewhere: RCSB PDB 1A4X · PDBe 1A4X · UniProt P39765
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