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Crystal structure of reduced ATFKBP13
Analyse Crystal structure of reduced ATFKBP13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y0O
- Type
- protein
- Length
- 625 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type peptidyl-prolyl cis-trans isomerase 3
- EC
- 5.2.1.8
- UniProt
- Q9SCY2
- Pockets
- 5 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Fkbp-type peptidyl-prolyl cis-trans isomerase 3 (EC 5.2.1.8) | protein | 125 | 9% helix, 43% strand | Q9SCY2 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.38 | 0.77 | 15 | empty |
| 2 | 78 | 0.38 | 0.77 | 15 | empty |
| 3 | 81 | 0.37 | 0.76 | 15 | empty |
| 4 | 82 | 0.35 | 0.75 | 14 | empty |
| 5 | 51 | 0.28 | 0.74 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–D · 631 Ų buried · 8 hydrogen bonds · protein-protein
- C–E · 629 Ų buried · 6 hydrogen bonds · protein-protein
- A–E · 251 Ų buried · 3 hydrogen bonds · protein-protein
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 Q9SCY2
- Elsewhere: RCSB PDB 1Y0O · PDBe 1Y0O · UniProt Q9SCY2
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