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Crystal structure of CLASP2 TOG1 domain
Analyse Crystal structure of CLASP2 TOG1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NR4
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clip-associating protein 2
- UniProt
- O75122
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clip-associating protein 2 | protein | 220 | 77% helix, 0% strand | O75122 |
| B | Clip-associating protein 2 | protein | 206 | 78% helix, 0% strand | O75122 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.51 | 0.75 | 36 | empty |
| 2 | 106 | 0.40 | 0.76 | 23 | empty |
| 3 | 68 | 0.29 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 911 Ų buried · 24 hydrogen bonds · protein-protein
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 O75122
- Elsewhere: RCSB PDB 5NR4 · PDBe 5NR4 · UniProt O75122
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