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Crystal Structure of human cyclic GMP-AMP synthase in complex with 5-(4-fluorophenyl)-2-methylpyrazole-3-carboxylic acid

Analyse Crystal Structure of human cyclic GMP-AMP synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FTI
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Homo sapiens
Molecule: Cyclic GMP-AMP synthase
EC: 2.7.7.86
UniProt: Q8N884
Ligands: YMI, ZN
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic GMP-AMP synthase (EC 2.7.7.86)	protein	354	42% helix, 17% strand	Q8N884

Ligands and binding sites

YMI · 3-(4-fluorophenyl)-1-methyl-1H-pyrazole-5-carboxylic acid · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

2 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	1169	0.77	0.79	90	YMI
2	73	0.34	0.76	18	empty

Compared structures

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 7FTI · PDBe 7FTI · UniProt Q8N884

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