Chlorine in PDB 9c8t: Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2

All present enzymatic activity of Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2:
2.7.7.86;

The structure of Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2, PDB code: 9c8t was solved by L.Wang, D.Sietsema, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.21 / 1.47
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	126.426, 51.972, 59.777, 90, 90, 90
R / Rfree (%)	18.6 / 21.2

The structure of Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2 also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2 (pdb code 9c8t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2, PDB code: 9c8t:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:99.8 occ:1.00 CL2 A:JUJ606 0.0 99.8 1.0 C14 A:JUJ606 1.8 14.7 1.0 C09 A:JUJ606 2.7 15.3 1.0 C16 A:JUJ606 2.7 15.7 1.0 N10 A:JUJ606 3.1 15.9 1.0 CL1 A:JUJ606 3.2 18.1 1.0 N1 A:ANP604 3.3 18.2 1.0 NH1 A:ARG376 3.3 35.6 1.0 CD A:ARG376 3.3 26.9 1.0 CZ A:ARG376 3.3 24.1 1.0 NE A:ARG376 3.4 27.6 1.0 C2 A:ANP604 3.4 17.6 1.0 CD A:LYS362 3.5 19.7 1.0 C6 A:ANP604 3.5 18.1 1.0 O A:HOH921 3.8 22.0 1.0 N3 A:ANP604 3.8 16.6 1.0 C5 A:ANP604 3.9 15.0 1.0 CE A:LYS362 4.0 29.0 1.0 C4 A:ANP604 4.0 16.1 1.0 NH2 A:ARG376 4.0 31.3 1.0 C18 A:JUJ606 4.0 14.1 1.0 C08 A:JUJ606 4.1 14.5 1.0 N6 A:ANP604 4.1 21.5 1.0 CG A:ARG376 4.3 25.5 1.0 C11 A:JUJ606 4.5 16.0 1.0 C19 A:JUJ606 4.6 13.9 1.0 N7 A:ANP604 4.8 16.0 1.0 CG A:LYS362 4.9 20.9 1.0 C07 A:JUJ606 4.9 15.4 1.0 N9 A:ANP604 5.0 15.3 1.0 O A:HOH782 5.0 27.8 1.0 NZ A:LYS362 5.0 33.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Cyclic Gmp-Amp Synthase in Complex with Amppnp and Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:18.1 occ:1.00 CL1 A:JUJ606 0.0 18.1 1.0 C16 A:JUJ606 1.7 15.7 1.0 C18 A:JUJ606 2.7 14.1 1.0 C14 A:JUJ606 2.7 14.7 1.0 O A:LEU377 3.1 17.0 0.6 O A:LEU377 3.2 17.0 0.5 CL2 A:JUJ606 3.2 99.8 1.0 CB A:SER378 3.6 16.2 1.0 O A:HOH815 3.6 21.2 1.0 CG A:ARG376 3.7 25.5 1.0 NE A:ARG376 3.7 27.6 1.0 O A:HOH782 3.7 27.8 1.0 N3 A:ANP604 3.7 16.6 1.0 C2 A:ANP604 3.8 17.6 1.0 CD A:ARG376 3.8 26.9 1.0 CA A:SER378 3.8 15.4 1.0 OG A:SER378 3.9 16.9 1.0 C A:LEU377 3.9 16.3 0.6 C19 A:JUJ606 3.9 13.9 1.0 C A:LEU377 3.9 16.3 0.5 C09 A:JUJ606 3.9 15.3 1.0 CG2 A:VAL360 4.0 15.4 1.0 N A:SER378 4.2 15.2 1.0 CZ A:ARG376 4.4 24.1 1.0 C08 A:JUJ606 4.5 14.5 1.0 CB A:ARG376 4.5 22.8 1.0 C4 A:ANP604 4.6 16.1 1.0 N1 A:ANP604 4.6 18.2 1.0 O A:ARG376 4.7 15.8 1.0 NH2 A:ARG376 4.8 31.3 1.0 C A:ARG376 4.8 16.8 1.0

A.M.Skeldon, L.Wang, N.Sgarioto, R.E.Beveridge, S.Chan, S.Dorich, V.Dumais, N.Fradet, S.Gaudreault, P.Legros, D.Mckay, R.Seliniotakis, D.V.Sietsema, L.Zhang, M.O.Boily, J.D.Burch, A.Caron, L.D.Fader, L.Lama, W.Xie, D.J.Patel, T.Tuschl, M.A.Crackower, K.A.Pike. Structural Insight Into the Cgas Active Site Explains Differences Between Therapeutically Relevant Species. Commun Chem V. 8 88 2025.
ISSN: ESSN 2399-3669
PubMed: 40121343
DOI: 10.1038/S42004-025-01481-7