Research workbench
Structural insight into the membrane insertion of tail-anchored proteins by GET3
Analyse Structural insight into the membrane insertion of tail-anchored proteins by GET3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A37
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATPase GET3
- EC
- 3.6.3.16
- UniProt
- Q12154
- Ligands
- ADP, ZN
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase GET3 (EC 3.6.3.16) | protein | 313 | 47% helix, 14% strand | Q12154 |
| B | ATPase GET3 (EC 3.6.3.16) | protein | 319 | 49% helix, 14% strand | Q12154 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1195 | 0.77 | 0.79 | 97 | ADP |
| 2 | 80 | 0.64 | 0.91 | 18 | empty |
| 3 | 149 | 0.61 | 0.84 | 26 | empty |
| 4 | 133 | 0.61 | 0.85 | 25 | empty |
| 5 | 91 | 0.53 | 0.84 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 739 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3A37 · Structural insight into the membrane insertion of tail-anchored proteins by Get3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q12154 · AlphaFold monomer V2.0 prediction for ATPase GET3 (Q12154) · a predicted model of the same protein · chain B against A, TM-score 0.85
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 Q12154
- Elsewhere: RCSB PDB 3A37 · PDBe 3A37 · UniProt Q12154
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