MolNFT v1 · #125866 · protein
Structure of the thermostabilized EAAT1 cryst-II mutant in complex with L-asp
5LLU · Excitatory amino acid transporter 1,NEUTRAL amino acid…: “Structure of the thermostabilized EAAT1 cryst-II mutant in complex with L-asp”. X-ray diffraction, 2 ligands (ASP, NA), 4 pockets (best druggability 0.65). MolNFT v1 #125866…
- PDB
- 5LLU
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Excitatory amino acid transporter 1,NEUTRAL amino acid transporter B(0),EXCITATORY amino…
- UniProt
- P43003, Q15758
- Ligands
- ASP, NA
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Excitatory amino acid transporter 1,NEUTRAL amino acid transporter B(0),EXCITATORY amino acid transporter 1 | protein | 396 | 82% helix, 1% strand | P43003, Q15758 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.65 | 0.79 | 38 | empty |
| 2 | 197 | 0.49 | 0.76 | 36 | empty |
| 3 | 125 | 0.47 | 0.78 | 17 | empty |
| 4 | 78 | 0.34 | 0.74 | 18 | empty |
Compared structures
- 5LLU · Structure of the thermostabilized EAAT1 cryst-II mutant in complex with L-ASP · the same entry in another collection · chain A against A, TM-score 1.00
- P43003 · AlphaFold monomer V2.0 prediction for excitatory amino acid transporter 1 (P43003) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q15758 · AlphaFold monomer V2.0 prediction for neutral amino acid transporter B(0) (Q15758) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P43003
- Every structure of UniProt Q15758
- Elsewhere: RCSB PDB 5LLU · PDBe 5LLU · UniProt P43003 · UniProt Q15758
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