Research workbench
A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in singal transduction
Analyse A transient interaction between two phosphorelay proteins trapped in a crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F51
- Type
- protein
- Length
- 1,202 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sporulation initiation phosphotransferase B; Sporulation initiation phosphotransferase F
- EC
- 2.7.-.-
- UniProt
- P06535, P06628
- Ligands
- MG
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Sporulation initiation phosphotransferase B (EC 2.7.-.-) | protein | 181 | 50% helix, 23% strand | P06535 |
| B, D | Sporulation initiation phosphotransferase B (EC 2.7.-.-) | protein | 182 | 47% helix, 23% strand | P06535 |
| E, F, G, H | Sporulation initiation phosphotransferase F (EC 2.7.-.-) | protein | 119 | 42% helix, 19% strand | P06628 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, E, B, F, D, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 697 | 0.80 | 0.84 | 70 | MG |
| 2 | 700 | 0.78 | 0.83 | 67 | MG |
| 3 | 623 | 0.78 | 0.83 | 64 | MG |
| 4 | 614 | 0.75 | 0.82 | 53 | empty |
| 5 | 295 | 0.70 | 0.84 | 31 | empty |
Interfaces
14 interfaces between chains.
- A–B · 1879 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 1847 Ų buried · 1 hydrogen bond · protein-protein
- B–F · 1069 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 1032 Ų buried · 13 hydrogen bonds · protein-protein
- D–H · 992 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1F51 · A transient interaction between two phosphorelay proteins trapped in a crystal lattice… · the same entry in another collection · chain H against H, TM-score 1.00
- P06628 · AlphaFold monomer V2.0 prediction for sporulation initiation phosphotransferase F (P06628) · a predicted model of the same protein · chain E against A, TM-score 0.98
- P06535 · AlphaFold monomer V2.0 prediction for sporulation initiation phosphotransferase B (P06535) · a predicted model of the same protein · chain A 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 P06535
- Every structure of UniProt P06628
- Elsewhere: RCSB PDB 1F51 · PDBe 1F51 · UniProt P06535 · UniProt P06628
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