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Crystal structure of mouse SEL1L
Analyse Crystal structure of mouse SEL1L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B26
- Type
- protein
- Length
- 689 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein sel-1 homolog 1
- UniProt
- Q9Z2G6
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Protein sel-1 homolog 1 | protein | 173 | 68% helix, 0% strand | Q9Z2G6 |
| B | Protein sel-1 homolog 1 | protein | 172 | 68% helix, 0% strand | Q9Z2G6 |
| C | Protein sel-1 homolog 1 | protein | 171 | 70% helix, 0% strand | Q9Z2G6 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 743 | 0.77 | 0.81 | 95 | empty |
| 2 | 527 | 0.70 | 0.79 | 57 | empty |
| 3 | 209 | 0.60 | 0.81 | 30 | empty |
| 4 | 243 | 0.58 | 0.79 | 33 | empty |
| 5 | 221 | 0.58 | 0.79 | 26 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1796 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1754 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 65 Ų buried · 1 hydrogen bond · 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 Q9Z2G6
- Elsewhere: RCSB PDB 5B26 · PDBe 5B26 · UniProt Q9Z2G6
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