Research workbench
Structure of apo FKBP12(P104G) from C. albicans
Analyse Structure of apo FKBP12(P104G) from C. albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5I98
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FK506-binding protein 1
- EC
- 5.2.1.8
- UniProt
- P28870
- Pockets
- 3 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FK506-binding protein 1 (EC 5.2.1.8) | protein | 120 | 8% helix, 37% strand | P28870 |
| B | FK506-binding protein 1 (EC 5.2.1.8) | protein | 119 | 8% helix, 37% strand | P28870 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.37 | 0.77 | 14 | empty |
| 2 | 60 | 0.36 | 0.77 | 12 | empty |
| 3 | 72 | 0.34 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 292 Ų buried · 4 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 P28870
- Elsewhere: RCSB PDB 5I98 · PDBe 5I98 · UniProt P28870
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