Research workbench
Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with SAFIT2
Analyse Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with SAFIT2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TXX
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- 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
- 37K
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8) | protein | 128 | 17% helix, 35% strand | Q13451 |
Ligands and binding sites
- 37K · (1R)-3-(3,4-dimethoxyphenyl)-1-{3-[2-(morpholin-4-yl)ethoxy]phenyl}propyl (2S)-1-[(2S)-2-[(1S)-cyclohex-2-en-1-yl]-2-(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.66 | 0.76 | 46 | 37K |
| 2 | 52 | 0.39 | 0.80 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 137 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6TXX · CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH SAFit2 · the same entry in another collection · chain B against B, 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 B 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 6TXX · PDBe 6TXX · UniProt Q13451
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