MolNFT v1 · #6190 · protein
A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in singal transduction
1F51: “A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism…”. X-ray diffraction. MolNFT v1 #6190 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1F51
- Type
- protein
- Length
- 1,202 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06535, P06628
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 181 | — | P06535 |
| B, D | — | protein | 182 | — | P06535 |
| E, F, G, H | — | protein | 119 | — | P06628 |
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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