Crystal structure of human wild type sting in complex with 2'-3'- cyclic-gmp-7-deaza-AMP

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 25% strand (DSSP).

Ligands and binding sites

• KT2 · 2-azanyl-9-[(1~{R},6~{R},8~{R},9~{R},10~{S},15~{R}, 17~{R},18~{R})-8-(4-azanylpyrrolo[2,3-d]pyrimidin-7-yl)-3,9,12,18-tetrakis(oxidanyl)-3,12-bis(oxidanylidene)-2,4,7,11,13,16-hexaoxa-3$L^{5}, 12$L^{5}-diphosphatricyclo[13.2.1.0^{6,10}]octadecan-17-yl]-1~{H}-purin-6-one · ligand · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2002 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

• 6S26 · Crystal structure of human wild type STING in complex with 2'-3'-cyclic-GMP-7-deaza-AMP · 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 A0A2R3XZB7
• Elsewhere: RCSB PDB 6S26 · PDBe 6S26 · UniProt A0A2R3XZB7