MolNFT v1 · #54475 · protein
Structure of the K294A mutant of vsglt
2XQ2 · SODIUM/GLUCOSE cotransporter: “Structure of the K294A mutant of vsglt”. X-ray diffraction, 12 pockets (best druggability 0.87). MolNFT v1 #54475 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2XQ2
- Type
- protein
- Length
- 1,060 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SODIUM/GLUCOSE cotransporter
- UniProt
- P96169
- Pockets
- 12 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SODIUM/GLUCOSE cotransporter | protein | 538 | 79% helix, 0% strand | P96169 |
| B | SODIUM/GLUCOSE cotransporter | protein | 522 | 78% helix, 0% strand | P96169 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.87 | 0.87 | 86 | empty |
| 2 | 1157 | 0.83 | 0.84 | 101 | PEG |
| 3 | 1017 | 0.81 | 0.82 | 85 | empty |
| 4 | 343 | 0.71 | 0.83 | 62 | PEG |
| 5 | 103 | 0.67 | 0.90 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1597 Ų buried · 19 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 P96169
- Elsewhere: RCSB PDB 2XQ2 · PDBe 2XQ2 · UniProt P96169
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