Research workbench
Inward-facing state of the glutamate transporter homologue gltph in complex with L-aspartate and sodium ions
Analyse Inward-facing state of the glutamate transporter homologue gltph in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X15
- Type
- protein
- Length
- 1,257 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate transporter homologue gltph
- Ligands
- 6OU, ASP, NA, HG
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate transporter homologue gltph | protein | 419 | 75% helix, 0% strand | — |
Ligands and binding sites
- 6OU · [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate · ligand · 39 copies · chains A, B, C
- ASP · Aspartic acid · ligand · 3 copies · chains A, B, C
- NA · Sodium ion · metal · 9 copies · chains A, B, C
- HG · Mercury (II) ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 695 | 0.88 | 0.91 | 40 | empty |
| 2 | 596 | 0.68 | 0.77 | 67 | empty |
| 3 | 315 | 0.63 | 0.79 | 38 | empty |
| 4 | 378 | 0.60 | 0.77 | 41 | empty |
| 5 | 326 | 0.60 | 0.78 | 47 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1109 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1105 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1101 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (formylation).
Compared structures
- 6X15 · Inward-facing state of the glutamate transporter homologue GltPh in complex with… · 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
- Elsewhere: RCSB PDB 6X15 · PDBe 6X15
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