Research workbench
Crystal structure of cryptosporidium parvum 14-3-3 protein in complex with peptide
Analyse Crystal structure of cryptosporidium parvum 14-3-3 protein in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NPM
- Type
- protein
- Length
- 484 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 domain containing protein; Consensus peptide for 14-3-3 proteins
- UniProt
- Q5CUW0
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 domain containing protein | protein | 237 | 83% helix, 0% strand | Q5CUW0 |
| X, Y | Consensus peptide for 14-3-3 proteins | protein | 6 | 0% helix, 0% strand | — |
| B | 14-3-3 domain containing protein | protein | 235 | 82% helix, 0% strand | Q5CUW0 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.54 | 0.75 | 25 | empty |
| 2 | 167 | 0.53 | 0.79 | 25 | empty |
| 3 | 152 | 0.49 | 0.78 | 25 | empty |
| 4 | 85 | 0.47 | 0.81 | 15 | empty |
| 5 | 82 | 0.46 | 0.81 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1092 Ų buried · 13 hydrogen bonds · protein-protein
- A–X · 448 Ų buried · 11 hydrogen bonds · protein-protein
- B–Y · 433 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2NPM · crystal structure of Cryptosporidium parvum 14-3-3 protein in complex with peptide · 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 Q5CUW0
- Elsewhere: RCSB PDB 2NPM · PDBe 2NPM · UniProt Q5CUW0
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