Research workbench
Crystal structure of a 14-3-3 protein from cryptosporidium parvum (CGD1_2980)
Analyse Crystal structure of a 14-3-3 protein from cryptosporidium parvum (CGD1_2980) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EFZ
- Type
- protein
- Length
- 869 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein
- UniProt
- Q5CSF3
- Pockets
- 12 · best druggability 0.68
Structure
x-ray diffraction · 4 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein | protein | 216 | 81% helix, 0% strand | Q5CSF3 |
| B | 14-3-3 protein | protein | 225 | 83% helix, 0% strand | Q5CSF3 |
| C | 14-3-3 protein | protein | 214 | 80% helix, 0% strand | Q5CSF3 |
| D | 14-3-3 protein | protein | 214 | 84% helix, 0% strand | Q5CSF3 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 581 | 0.68 | 0.78 | 47 | empty |
| 2 | 597 | 0.66 | 0.76 | 48 | empty |
| 3 | 186 | 0.49 | 0.76 | 22 | empty |
| 4 | 91 | 0.44 | 0.79 | 17 | empty |
| 5 | 68 | 0.44 | 0.81 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1835 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1805 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 441 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3EFZ · Crystal Structure of a 14-3-3 protein from cryptosporidium parvum (cgd1_2980) · 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 Q5CSF3
- Elsewhere: RCSB PDB 3EFZ · PDBe 3EFZ · UniProt Q5CSF3
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