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Structure of apo P1 form of Candida albicans FKBP12
Analyse Structure of apo P1 form of Candida albicans FKBP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HTG
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Candida albicans (strain SC5314 / ATCC MYA-2876)
- Molecule
- FK506-binding protein 1
- EC
- 5.2.1.8
- UniProt
- P28870
- Pockets
- 5 · best druggability 0.49
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | FK506-binding protein 1 (EC 5.2.1.8) | protein | 122 | 15% helix, 36% strand | P28870 |
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 | 161 | 0.49 | 0.78 | 42 | empty |
| 2 | 61 | 0.36 | 0.79 | 15 | empty |
| 3 | 74 | 0.35 | 0.76 | 17 | empty |
| 4 | 57 | 0.33 | 0.76 | 14 | empty |
| 5 | 53 | 0.31 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 688 Ų buried · 11 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 5HTG · PDBe 5HTG · UniProt P28870
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