Structure of a human NHE3-CHP1 complex in the autoinhibited state

Structure

electron microscopy · 3 distinct chains · 70% helix, 1% strand (DSSP).

Ligands and binding sites

• PGT · (1S)-2-{[{[(2R)-2,3-dihydroxypropyl]oxy}(hydroxy) phosphoryl]oxy}-1-[(palmitoyloxy)methyl]ethyl stearate · ligand · 10 copies · chains A, B
• 85R · [(2~{R})-2-hexadecanoyloxy-3-[oxidanyl-[(2~{S},3~{S}, 5~{R},6~{S})-2,3,4,5,6-pentakis(oxidanyl) cyclohexyl]oxy-phosphoryl]oxy-propyl] hexadecanoate · ligand · 2 copies · chains A, C, B, D

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

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 3072 Ų buried · 10 hydrogen bonds · protein-protein
• A–C · 2413 Ų buried · 22 hydrogen bonds · protein-protein
• B–D · 2304 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

• 7X2U · Structure of a human NHE3-CHP1 complex in the autoinhibited state · the same entry in another collection · chain C against C, TM-score 1.00
• Q99653 · AlphaFold monomer V2.0 prediction for calcineurin B homologous protein 1 (Q99653) · a predicted model of the same protein · chain D against A, TM-score 0.94
• P48764 · AlphaFold monomer V2.0 prediction for SODIUM/HYDROGEN exchanger 3 (P48764) · a predicted model of the same protein · chain B against A, TM-score 0.83

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 P48764
• Every structure of UniProt Q99653
• Elsewhere: RCSB PDB 7X2U · PDBe 7X2U · UniProt P48764 · UniProt Q99653