Research workbench
Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)
Analyse Complex between YPD1 and SLN1 response regulator domain in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OXB
- Type
- protein
- Length
- 290 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- YPD1P; SLN1
- EC
- 2.7.3.-
- UniProt
- Q07688, P39928
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | YPD1P | protein | 166 | 62% helix, 0% strand | Q07688 |
| B | SLN1 (EC 2.7.3.-) | protein | 124 | 43% helix, 19% strand | P39928 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.44 | 0.79 | 19 | empty |
| 2 | 69 | 0.39 | 0.79 | 17 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1001 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1OXB · Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1) · the same entry in another collection · chain A against A, TM-score 1.00
- P39928 · AlphaFold monomer V2.0 prediction for osmosensing histidine protein kinase SLN1 (P39928) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q07688 · AlphaFold monomer V2.0 prediction for phosphorelay intermediate protein YPD1 (Q07688) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q07688
- Every structure of UniProt P39928
- Elsewhere: RCSB PDB 1OXB · PDBe 1OXB · UniProt Q07688 · UniProt P39928
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