Research workbench
Crystal structure of human FKBD25 in complex with FK506
Analyse Crystal structure of human FKBD25 in 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
- 5D75
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP3
- EC
- 5.2.1.8
- UniProt
- Q00688
- Ligands
- JEF, FK5
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP3 (EC 5.2.1.8) | protein | 120 | 8% helix, 37% strand | Q00688 |
Ligands and binding sites
- JEF · O-(O-(2-aminopropyl)-O'-(2-methoxyethyl)polypropylene glycol 500) · ligand · 2 copies · chains A
- FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · 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 | 70 | 0.37 | 0.77 | 14 | empty |
Compared structures
- 5D75 · Crystal structure of Human FKBD25 in complex with FK506 · the same entry in another collection · chain A against A, TM-score 1.00
- Q00688 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP3 (Q00688) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q00688
- Elsewhere: RCSB PDB 5D75 · PDBe 5D75 · UniProt Q00688
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