Research workbench
Fkbp-rapamycin binding domain (frb) of the fkbp-rapamycin associated protein
Analyse Fkbp-rapamycin binding domain (frb) of the fkbp-rapamycin associated protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AUE
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-rapamycin associated protein
- UniProt
- P42345
Structure
x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbp-rapamycin associated protein | protein | 92 | 84% helix, 0% strand | P42345 |
| B | Fkbp-rapamycin associated protein | protein | 94 | 84% helix, 0% strand | P42345 |
Interfaces
1 interface between chains.
- A–B · 15 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1AUE · Fkbp-rapamycin binding domain (frb) of the fkbp-rapamycin associated protein · the same entry in another collection · chain A against A, TM-score 1.00
- P42345 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase mtor (P42345) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P42345
- Elsewhere: RCSB PDB 1AUE · PDBe 1AUE · UniProt P42345
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