Research workbench
X-ray structure of leut with V269 deletion
Analyse X-ray structure of leut with V269 deletion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NLE
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NA(+):NEUROTRANSMITTER symporter (snf family)
- UniProt
- O67854
- Ligands
- LEU, NA
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NA(+):NEUROTRANSMITTER symporter (snf family) | protein | 491 | 78% helix, 1% strand | O67854 |
Ligands and binding sites
- LEU · Leucine · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
- OCT · N-octane · additive · 2 copies · chains A
- BOG · octyl beta-D-glucopyranoside · additive · chains A
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 | 389 | 0.67 | 0.80 | 47 | empty |
| 2 | 89 | 0.46 | 0.79 | 16 | empty |
| 3 | 50 | 0.40 | 0.81 | 12 | empty |
| 4 | 52 | 0.29 | 0.74 | 11 | empty |
Compared structures
- 6NLE · X-ray structure of LeuT with V269 deletion · 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
- Every structure of UniProt O67854
- Elsewhere: RCSB PDB 6NLE · PDBe 6NLE · UniProt O67854
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