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The cryoem structure of human gamma-secretase complex
Analyse The cryoem structure of human gamma-secretase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UIS
- Type
- protein
- Length
- 1,249 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-secretase; Lysozyme
- EC
- 3.2.1.17
- UniProt
- A0A097J809
- Pockets
- 18 · best druggability 0.80
Structure
electron microscopy · 5 distinct chains · 54% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-secretase | protein | 588 | 29% helix, 13% strand | — |
| B | Gamma-secretase | protein | 241 | 85% helix, 0% strand | — |
| C | Gamma-secretase | protein | 196 | 79% helix, 0% strand | — |
| D | Gamma-secretase | protein | 62 | 84% helix, 0% strand | — |
| G | Lysozyme (EC 3.2.1.17) | protein | 162 | 57% helix, 6% strand | A0A097J809 |
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1157 | 0.80 | 0.81 | 134 | empty |
| 2 | 676 | 0.71 | 0.78 | 82 | empty |
| 3 | 367 | 0.70 | 0.82 | 37 | empty |
| 4 | 65 | 0.67 | 0.94 | 23 | empty |
| 5 | 90 | 0.58 | 0.86 | 25 | empty |
Interfaces
4 interfaces between chains.
- B–C · 803 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 411 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 203 Ų buried · 2 hydrogen bonds · protein-protein
- B–G · 17 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4UIS · The cryoEM structure of human gamma-Secretase complex · 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 A0A097J809
- Elsewhere: RCSB PDB 4UIS · PDBe 4UIS · UniProt A0A097J809
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