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Structure of glutamate transporter homologue GltTk in the presence of TBOA inhibitor

Analyse Structure of glutamate transporter homologue GltTk in the presence of TBOA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XWN
Type
protein
Length
1,276 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.47
Source
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Molecule
Proton/glutamate symporter, SDF family
UniProt
Q5JID0
Ligands
TB1
Pockets
15 · best druggability 0.88

Structure

electron microscopy · resolution 3.47 · 3 distinct chains · 70% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProton/glutamate symporter, SDF familyprotein42772% helix, 0% strandQ5JID0
BProton/glutamate symporter, SDF familyprotein42672% helix, 0% strandQ5JID0
CProton/glutamate symporter, SDF familyprotein42365% helix, 0% strandQ5JID0

Ligands and binding sites

  • TB1 · (3S)-3-(benzyloxy)-L-aspartic acid · ligand · 2 copies · chains B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15170.880.9337empty
24750.660.7856TB1
33520.630.7941TB1
42870.610.7945empty
53510.560.7435empty

Interfaces

3 interfaces between chains.

  • A–B · 1210 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1190 Ų buried · 13 hydrogen bonds · protein-protein
  • A–C · 1179 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 6XWN · Structure of glutamate transporter homologue glttk in the presence of tboa inhibitor · the same entry in another collection · chain A against A, TM-score 1.00

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