Research workbench
Crystal structure analysis of FKBP52, complex with FK506
Analyse Crystal structure analysis of FKBP52, complex with FK506 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LAX
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP4
- EC
- 5.2.1.8
- UniProt
- Q02790
- Ligands
- FK5
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP4 (EC 5.2.1.8) | protein | 237 | 13% helix, 40% strand | Q02790 |
Ligands and binding sites
- FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
- GOL · Glycerol · additive · 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 | 72 | 0.40 | 0.78 | 13 | empty |
Compared structures
- 4LAX · Crystal Structure Analysis of FKBP52, Complex with FK506 · the same entry in another collection · chain A against A, TM-score 1.00
- Q02790 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP4 (Q02790) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q02790
- Elsewhere: RCSB PDB 4LAX · PDBe 4LAX · UniProt Q02790
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