Research workbench
HEAAT3-asymmetric-1O2I
Analyse HEAAT3-asymmetric-1O2I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X3E
- Type
- protein
- Length
- 1,241 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Excitatory amino acid transporter 3
- UniProt
- P43005
- Ligands
- ASP, NA
- Pockets
- 18 · best druggability 0.88
Structure
electron microscopy · 2 distinct chains · 71% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Excitatory amino acid transporter 3 | protein | 419 | 70% helix, 4% strand | P43005 |
| B, C | Excitatory amino acid transporter 3 | protein | 411 | 72% helix, 3% strand | P43005 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.88 | 0.88 | 49 | empty |
| 2 | 282 | 0.76 | 0.88 | 38 | empty |
| 3 | 286 | 0.75 | 0.87 | 42 | empty |
| 4 | 876 | 0.74 | 0.78 | 79 | empty |
| 5 | 722 | 0.70 | 0.77 | 84 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1437 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 1412 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1412 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
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 P43005
- Elsewhere: RCSB PDB 6X3E · PDBe 6X3E · UniProt P43005
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