MolNFT v1 · #12830 · protein
Structure of the large fkbp-like protein, FKBP51, involved in steroid receptor complexes
1KT1 · FK506-binding protein FKBP51: “Structure of the large fkbp-like protein, FKBP51, involved in steroid receptor complexes”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.43). MolNFT v1 #12830 on GenesisL1: 3D…
- PDB
- 1KT1
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FK506-binding protein FKBP51
- EC
- 5.2.1.8
- UniProt
- Q9XSH5
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FK506-binding protein FKBP51 (EC 5.2.1.8) | protein | 374 | 41% helix, 20% strand | Q9XSH5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.43 | 0.82 | 21 | empty |
| 2 | 167 | 0.42 | 0.73 | 25 | empty |
| 3 | 129 | 0.38 | 0.73 | 22 | empty |
Compared structures
- 1KT1 · Structure of the Large FKBP-like Protein, FKBP51, Involved in Steroid Receptor Complexes · the same entry in another collection · chain A against A, TM-score 1.00
- Q9XSH5 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q9XSH5) · 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 Q9XSH5
- Elsewhere: RCSB PDB 1KT1 · PDBe 1KT1 · UniProt Q9XSH5
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