Research workbench
The FK1 domain of FKBP51 in complex with ((1S,5S,6R)-10-((3,5- DICHLOROPHENYL)SULFONYL)-2-oxo-5-vinyl-3,10-DIAZABICYCLO[4.3.1]DECAN- 3-YL)ACETIC acid
Analyse The FK1 domain of FKBP51 in complex with ((1S,5S,6R)-10-((3,5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7APT
- Type
- protein
- Length
- 127 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
- RRZ
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8) | protein | 127 | 17% helix, 36% strand | Q13451 |
Ligands and binding sites
- RRZ · 2-[(1~{S},5~{S},6~{R})-10-[3,5-bis(chloranyl) phenyl]sulfonyl-5-ethenyl-2-oxidanylidene-3,10-diazabicyclo[4.3.1]decan-3-yl]ethanoic acid · 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 | 78 | 0.41 | 0.78 | 14 | RRZ |
Compared structures
- 7APT · The Fk1 domain of FKBP51 in complex with ((1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-2-o… · 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 7APT · PDBe 7APT · UniProt Q13451
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