Research workbench
Crystal structure of FKBP52 C-terminal domain
Analyse Crystal structure of FKBP52 C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P5Q
- Type
- protein
- Length
- 849 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FK506-binding protein 4
- EC
- 5.2.1.8
- UniProt
- Q02790
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | FK506-binding protein 4 (EC 5.2.1.8) | protein | 283 | 54% helix, 17% strand | Q02790 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.72 | 0.84 | 30 | empty |
| 2 | 356 | 0.71 | 0.83 | 32 | empty |
| 3 | 385 | 0.57 | 0.75 | 39 | SO4 |
| 4 | 123 | 0.41 | 0.75 | 23 | empty |
| 5 | 136 | 0.39 | 0.73 | 20 | SO4 |
Interfaces
2 interfaces between chains.
- A–C · 1031 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 809 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
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 1P5Q · PDBe 1P5Q · UniProt Q02790
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.