Research workbench
Yeast-specific SERINE/THREONINE protein phosphatase (PPZ1) of candida albicans
Analyse Yeast-specific SERINE/THREONINE protein phosphatase (PPZ1) of candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JPE
- Type
- protein
- Length
- 617 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase
- EC
- 3.1.3.16
- UniProt
- C4YM68
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein phosphatase (EC 3.1.3.16) | protein | 310 | 37% helix, 18% strand | C4YM68 |
| B | SERINE/THREONINE-protein phosphatase (EC 3.1.3.16) | protein | 307 | 38% helix, 18% strand | C4YM68 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.80 | 0.83 | 116 | FLC |
| 2 | 182 | 0.65 | 0.85 | 36 | GOL |
| 3 | 222 | 0.60 | 0.81 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1340 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5JPE · Yeast-specific serine/threonine protein phosphatase (PPZ1) of Candida albicans · the same entry in another collection · chain A against A, TM-score 1.00
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 C4YM68
- Elsewhere: RCSB PDB 5JPE · PDBe 5JPE · UniProt C4YM68
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