Research workbench
Inward-facing structure of human EAAT2 in the substrate-free state
Analyse Inward-facing structure of human EAAT2 in the substrate-free state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VR8
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Excitatory amino acid transporter 2
- UniProt
- P43004
- Ligands
- PC1, 9Z9, CLR
- Pockets
- 6 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 80% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Excitatory amino acid transporter 2 | protein | 402 | 80% helix, 3% strand | P43004 |
Ligands and binding sites
- PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A
- 9Z9 · (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en · ligand · chains A
- CLR · Cholesterol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.72 | 0.82 | 41 | empty |
| 2 | 378 | 0.66 | 0.79 | 33 | 9Z9 |
| 3 | 123 | 0.58 | 0.85 | 24 | empty |
| 4 | 86 | 0.36 | 0.75 | 14 | empty |
| 5 | 80 | 0.36 | 0.75 | 17 | empty |
Compared structures
- 7VR8 · Inward-facing structure of human EAAT2 in the substrate-free state · the same entry in another collection · chain A against A, TM-score 1.00
- P43004 · AlphaFold monomer V2.0 prediction for excitatory amino acid transporter 2 (P43004) · a predicted model of the same protein · chain A against A, TM-score 0.63
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 P43004
- Elsewhere: RCSB PDB 7VR8 · PDBe 7VR8 · UniProt P43004
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