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Human cyclic gmp-AMP synthase (cgas) in complex with sulfate ion

Analyse Human cyclic gmp-AMP synthase (cgas) in complex with sulfate ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O69
Type: protein
Length: 353 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic gmp-AMP synthase
EC: 2.7.7.86
UniProt: Q8N884
Ligands: ZN, SO4
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic gmp-AMP synthase (EC 2.7.7.86)	protein	353	44% helix, 17% strand	Q8N884

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	775	0.75	0.80	57	SO4
2	167	0.49	0.77	26	SO4
3	154	0.46	0.76	25	empty
4	68	0.35	0.76	14	empty
5	58	0.26	0.73	14	empty

Compared structures

4O69 · Human cyclic GMP-AMP synthase (cGAS) in complex with sulfate ion · the same entry in another collection · chain A against A, TM-score 1.00
Q8N884 · AlphaFold monomer V2.0 prediction for cyclic gmp-AMP synthase (Q8N884) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8N884
Elsewhere: RCSB PDB 4O69 · PDBe 4O69 · UniProt Q8N884

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