Zinc in PDB 6w2j: CPS1 Bound to Allosteric Inhibitor H3B-374

All present enzymatic activity of CPS1 Bound to Allosteric Inhibitor H3B-374:
6.3.4.16;

The structure of CPS1 Bound to Allosteric Inhibitor H3B-374, PDB code: 6w2j was solved by N.A.Larsen, T.V.Nguyen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.96 / 2.62
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	71.66, 98.53, 142.53, 102.13, 97.94, 106.11
R / Rfree (%)	19 / 25

The structure of CPS1 Bound to Allosteric Inhibitor H3B-374 also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Zinc atom in the CPS1 Bound to Allosteric Inhibitor H3B-374 (pdb code 6w2j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the CPS1 Bound to Allosteric Inhibitor H3B-374, PDB code: 6w2j:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the CPS1 Bound to Allosteric Inhibitor H3B-374


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of CPS1 Bound to Allosteric Inhibitor H3B-374 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1602 b:60.3 occ:1.00 OE2 A:GLU362 1.8 65.7 1.0 OD1 A:ASN315 2.0 54.3 1.0 OE1 A:GLN335 2.1 41.3 1.0 NE2 A:HIS337 2.2 50.8 1.0 CD A:GLU362 2.5 61.0 1.0 OE1 A:GLU362 2.6 62.4 1.0 CG A:ASN315 2.9 42.2 1.0 CE1 A:HIS337 3.0 50.2 1.0 CD A:GLN335 3.1 42.9 1.0 CB A:ASN315 3.3 42.0 1.0 CD2 A:HIS337 3.4 50.4 1.0 NE2 A:GLN335 3.5 40.5 1.0 ND2 A:ASN355 3.8 57.4 1.0 CG A:GLN375 3.9 51.2 1.0 CG A:GLU362 4.0 58.9 1.0 ND2 A:ASN315 4.0 43.5 1.0 OG1 A:THR360 4.1 53.8 1.0 CE A:MET311 4.2 48.4 1.0 ND1 A:HIS337 4.2 45.9 1.0 CG A:HIS337 4.4 47.0 1.0 CG A:GLN335 4.5 40.9 1.0 O A:ASN361 4.5 55.6 1.0 CB A:GLN375 4.7 52.9 1.0 CA A:ASN315 4.8 41.1 1.0 CB A:GLN335 4.8 39.4 1.0 CG A:ASN355 5.0 60.0 1.0 CB A:GLU362 5.0 55.1 1.0

Zinc binding site 2 out of 2 in the CPS1 Bound to Allosteric Inhibitor H3B-374


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of CPS1 Bound to Allosteric Inhibitor H3B-374 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1602 b:74.5 occ:1.00 OE2 B:GLU362 1.8 72.9 1.0 OE1 B:GLN335 2.0 45.2 1.0 NE2 B:HIS337 2.3 51.0 1.0 CD B:GLU362 2.4 70.3 1.0 OE1 B:GLU362 2.4 74.9 1.0 OD1 B:ASN315 2.6 61.9 1.0 CD B:GLN335 3.0 46.5 1.0 CG B:ASN315 3.1 51.6 1.0 CD2 B:HIS337 3.2 50.6 1.0 CE1 B:HIS337 3.3 54.0 1.0 NE2 B:GLN335 3.5 47.6 1.0 CB B:ASN315 3.6 53.8 1.0 ND2 B:ASN315 3.9 54.6 1.0 CG B:GLU362 3.9 68.7 1.0 ND2 B:ASN355 3.9 68.3 1.0 CG B:GLN375 4.0 59.9 1.0 OG1 B:THR360 4.1 56.0 1.0 CG B:GLN335 4.4 45.8 1.0 CG B:HIS337 4.4 53.9 1.0 ND1 B:HIS337 4.4 49.9 1.0 O B:ASN361 4.6 74.4 1.0 CE B:MET311 4.7 71.8 1.0 CB B:GLN375 4.8 59.4 1.0 CB B:GLN335 4.9 43.2 1.0 CB B:GLU362 5.0 63.6 1.0 CG B:ASN355 5.0 73.4 1.0

A.Rolfe, S.Yao, T.V.Nguyen, K.Omoto, F.Colombo, M.Virrankoski, F.H.Vaillancourt, L.Yu, A.Cook, D.Reynolds, S.Ioannidis, P.Zhu, N.A.Larsen, D.M.Bolduc. Discovery of 2,6-Dimethylpiperazines As Allosteric Inhibitors of CPS1. Acs Med.Chem.Lett. V. 11 1305 2020.
ISSN: ISSN 1948-5875
PubMed: 32551016
DOI: 10.1021/ACSMEDCHEMLETT.0C00145