Research workbench
Domain-swapping in the sporulation response regulator SPO0A
Analyse Domain-swapping in the sporulation response regulator SPO0A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DZ3
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stage 0 sporulation protein a
- UniProt
- P52934
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stage 0 sporulation protein a | protein | 123 | 43% helix, 24% strand | P52934 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.39 | 0.73 | 21 | empty |
Compared structures
- 1DZ3 · Domain-swapping in the sporulation response regulator SPO0A · the same entry in another collection · chain A against A, TM-score 1.00
- P52934 · AlphaFold monomer V2.0 prediction for stage 0 sporulation protein a (P52934) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P52934
- Elsewhere: RCSB PDB 1DZ3 · PDBe 1DZ3 · UniProt P52934
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