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Crystal structure of HSTING(H232) in complex with C[G(2',5')PA(3',5') P]

Analyse Crystal structure of HSTING(H232) in complex with C[G(2',5')PA(3',5') P] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LOH
Type: protein
Length: 368 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stimulator of interferon genes protein
UniProt: Q86WV6
Ligands: 1SY
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Stimulator of interferon genes protein	protein	184	42% helix, 24% strand	Q86WV6

Ligands and binding sites

1SY · cGAMP · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	373	0.82	0.91	47	1SY

Interfaces

1 interface between chains.

A–B · 1932 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

4LOH · Crystal structure of hSTING(H232) in complex with c[G(2',5')pA(3',5')p] · 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 4LOH · PDBe 4LOH · UniProt Q86WV6

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