MolNFT v1 · #96297 · protein
Increasing the efficiency efficiency of ligands for the FK506-binding protein 51 by conformational control: complex of FKBP51 with 2-(3,4- DIMETHOXYPHENOXY)ETHYL (2S)-1-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6- YL)SULFONYL]PIPERIDINE-2-carboxylate
4JFM · Peptidyl-prolyl cis-trans isomerase FKBP5: “Increasing the efficiency efficiency of ligands for the FK506-binding protein 51 by conformational control…”. X-ray diffraction, 1 ligand (1KZ), 1 pocket (best druggability 0.43). MolNFT…
- PDB
- 4JFM
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP5
- EC
- 5.2.1.8
- UniProt
- Q13451
- Ligands
- 1KZ
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8) | protein | 128 | 16% helix, 36% strand | Q13451 |
Ligands and binding sites
- 1KZ · 2-(3,4-dimethoxyphenoxy)ethyl (2S)-1-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6-yl)sulfonyl]piperidine-2-carboxylate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.43 | 0.78 | 16 | 1KZ |
Compared structures
- 4JFM · Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q13451
- Elsewhere: RCSB PDB 4JFM · PDBe 4JFM · UniProt Q13451
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.