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Cryoem structure of SGLT1 at 3.4 a resolution

Analyse Cryoem structure of SGLT1 at 3.4 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7SL8
Type
protein
Length
700 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SODIUM/GLUCOSE cotransporter 1; Nanobody NB1
Ligands
CLR
Pockets
7 · best druggability 0.72

Structure

electron microscopy · 2 distinct chains · 56% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASODIUM/GLUCOSE cotransporter 1protein58267% helix, 2% strand—
BNanobody NB1protein1180% helix, 38% strand—

Ligands and binding sites

  • CLR · Cholesterol · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.720.9718empty
25670.680.7857empty
32660.620.8143empty
4910.510.8218empty
5660.430.8121empty

Interfaces

1 interface between chains.

  • A–B · 737 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 7SL8 · CryoEM structure of SGLT1 at 3.4 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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