Research workbench
Crystal structure of GET3
Analyse Crystal structure of GET3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H84
- Type
- protein
- Length
- 649 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
- NA, MG, ZN, CL
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase GET3 (EC 3.6.3.16) | protein | 326 | 49% helix, 14% strand | Q12154 |
| B | ATPase GET3 (EC 3.6.3.16) | protein | 323 | 49% helix, 13% strand | Q12154 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ZN · Zinc ion · metal · chains A, B
- CL · Chloride ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1103 | 0.78 | 0.80 | 93 | MG |
| 2 | 56 | 0.67 | 0.95 | 17 | NA |
| 3 | 97 | 0.61 | 0.88 | 19 | CL |
| 4 | 99 | 0.57 | 0.85 | 21 | CL |
| 5 | 122 | 0.56 | 0.83 | 25 | NA |
Interfaces
1 interface between chains.
- A–B · 874 Ų buried · 7 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 Q12154
- Elsewhere: RCSB PDB 3H84 · PDBe 3H84 · UniProt Q12154
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