Research workbench
Structure of glutamate transporter homologue GltTk in the saturated conditions
Analyse Structure of glutamate transporter homologue GltTk in the saturated conditions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XWQ
- Type
- protein
- Length
- 1,278 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.41
- Source
- Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
- Molecule
- Proton/glutamate symporter, SDF family
- UniProt
- Q5JID0
- Ligands
- ASP
- Pockets
- 18 · best druggability 0.88
Structure
electron microscopy · resolution 3.41 · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Proton/glutamate symporter, SDF family | protein | 426 | 72% helix, 0% strand | Q5JID0 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 525 | 0.88 | 0.93 | 37 | empty |
| 2 | 607 | 0.67 | 0.76 | 69 | empty |
| 3 | 376 | 0.65 | 0.79 | 49 | empty |
| 4 | 311 | 0.62 | 0.78 | 44 | empty |
| 5 | 386 | 0.61 | 0.76 | 46 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1217 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1216 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 1212 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6XWQ · Structure of glutamate transporter homologue glttk in the saturated conditions · 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 Q5JID0
- Elsewhere: RCSB PDB 6XWQ · PDBe 6XWQ · UniProt Q5JID0
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