MolNFT v1 · #169110 · protein
Inward-facing state of the glutamate transporter homologue gltph in complex with L-aspartate and sodium ions
6X15: “Inward-facing state of the glutamate transporter homologue gltph in complex with L-aspartate and sodium ions”. Electron microscopy, 3 ligands (6OU, NA, HG). MolNFT v1 #169110 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6X15
- Type
- protein
- Length
- 1,260 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- 6OU, NA, HG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 420 | — | — |
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
- 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.
Compared structures
- 6X15 · Inward-facing state of the glutamate transporter homologue GltPh in complex with… · the same entry in another collection · chain B against B, 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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