MolNFT v1 · #97678 · protein

X-ray crystal structure of human cyclic gmp-AMP synthase (cgas)

4KM5: “X-ray crystal structure of human cyclic gmp-AMP synthase (cgas)”. X-ray diffraction, 1 ligand (ZN), 7 pockets (best druggability 0.77). MolNFT v1 #97678 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4KM5
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic gmp-AMP synthase
EC: 2.7.7.-
UniProt: Q8N884
Ligands: ZN
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic gmp-AMP synthase (EC 2.7.7.-)	protein	362	43% helix, 16% strand	Q8N884

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	746	0.77	0.81	53	empty
2	278	0.68	0.83	26	empty
3	107	0.44	0.78	24	empty
4	56	0.34	0.78	17	empty
5	66	0.33	0.76	19	empty

Compared structures

4KM5 · X-ray crystal structure of human cyclic GMP-AMP synthase (cGAS) · 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 0.96

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 4KM5 · PDBe 4KM5 · UniProt Q8N884

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.