Research workbench
Candida albicans PKh Kinase Domain
Analyse Candida albicans PKh Kinase Domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C0T
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.16
- Source
- CANDIDA ALBICANS
- Molecule
- Likely protein kinase
- EC
- 2.7.11.1
- UniProt
- Q5A3P6
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · resolution 3.16 · 1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Likely protein kinase (EC 2.7.11.1) | protein | 291 | 36% helix, 16% strand | Q5A3P6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.69 | 0.80 | 42 | empty |
| 2 | 80 | 0.34 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 Q5A3P6
- Elsewhere: RCSB PDB 4C0T · PDBe 4C0T · UniProt Q5A3P6
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