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Structure of human sting in complex with mk-1454

Analyse Structure of human sting in complex with mk-1454 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MHC
Type: protein
Length: 179 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q86WV6
Ligands: ZEV

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	179	—	Q86WV6

Ligands and binding sites

ZEV · (2r,5r,7r,8s,10r,12ar,14r,15s,15ar,16r)-7-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-14-(6-amino-9H-purin-9-yl)-15,16-difluoro-2,10-bis(sulfanyl)octahydro-2H,10H, 12H-5,8-methano-2lambda~5~,10lambda~5~-furo[3,2-L][1, 3,6,9,11,2,10]pentaoxadiphosphacyclotetradecine-2,10-dione · ligand · chains A

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

Compared structures

7MHC · Structure of human STING in complex with MK-1454 · the same entry in another collection · chain A against A, TM-score 1.00
Q86WV6 · AlphaFold monomer V2.0 prediction for stimulator of interferon genes protein (Q86WV6) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q86WV6
Elsewhere: RCSB PDB 7MHC · PDBe 7MHC · UniProt Q86WV6

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