Research workbench
Crystal structure of the pryspry-domain
Analyse Crystal structure of the pryspry-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FBE
- Type
- protein
- Length
- 775 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted: similar to ret finger protein-like 1
- Pockets
- 11 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 3% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Predicted: similar to ret finger protein-like 1 | protein | 188 | 2% helix, 40% strand | — |
| B | Predicted: similar to ret finger protein-like 1 | protein | 198 | 4% helix, 36% strand | — |
| C | Predicted: similar to ret finger protein-like 1 | protein | 199 | 4% helix, 36% strand | — |
| D | Predicted: similar to ret finger protein-like 1 | protein | 190 | 3% helix, 39% strand | — |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.55 | 0.79 | 33 | empty |
| 2 | 210 | 0.55 | 0.78 | 36 | empty |
| 3 | 212 | 0.53 | 0.78 | 37 | empty |
| 4 | 241 | 0.53 | 0.76 | 30 | empty |
| 5 | 156 | 0.52 | 0.80 | 29 | empty |
Interfaces
4 interfaces between chains.
- C–D · 671 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 645 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 362 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 344 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2FBE · Crystal Structure of the PRYSPRY-domain · the same entry in another collection · chain C against C, 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
- Elsewhere: RCSB PDB 2FBE · PDBe 2FBE
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