Research workbench
Mouse gamma S crystallin L16 octamer
Analyse Mouse gamma S crystallin L16 octamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RJ0
- Type
- protein
- Length
- 707 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-crystallin S
- UniProt
- O35486
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C | Gamma-crystallin S | protein | 177 | 9% helix, 38% strand | O35486 |
| D | Gamma-crystallin S | protein | 176 | 2% helix, 37% strand | O35486 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.78 | 0.81 | 79 | empty |
| 2 | 179 | 0.74 | 0.91 | 34 | empty |
| 3 | 551 | 0.71 | 0.80 | 65 | empty |
| 4 | 301 | 0.63 | 0.80 | 37 | empty |
| 5 | 58 | 0.52 | 0.87 | 18 | empty |
Interfaces
5 interfaces between chains.
- B–A · 1237 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1158 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 529 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 360 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 327 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified, 2 disulfide (engineered, disulfide).
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 O35486
- Elsewhere: RCSB PDB 7RJ0 · PDBe 7RJ0 · UniProt O35486
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