Chlorine in PDB 5dou: Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form

All present enzymatic activity of Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form:
6.3.4.16;

The structure of Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form, PDB code: 5dou was solved by S.De Cima, L.M.Polo, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	78.919, 98.558, 214.890, 90.66, 98.65, 90.08
R / Rfree (%)	19.5 / 22.9

The structure of Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form also contains other interesting chemical elements:

Nickel	(Ni)	4 atoms
Magnesium	(Mg)	12 atoms
Potassium	(K)	18 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form (pdb code 5dou). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form, PDB code: 5dou:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form


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 Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl2012 b:31.3 occ:1.00 O A:HOH2320 3.2 39.6 1.0 O A:HOH2327 3.2 29.1 1.0 N A:ARG1262 3.5 24.9 1.0 NH1 A:ARG1259 3.6 40.0 1.0 CA A:SER1261 3.6 24.2 1.0 CB A:SER1261 3.7 24.6 1.0 O A:HOH2319 3.8 38.1 1.0 NH1 A:ARG1262 3.8 28.8 1.0 CZ A:ARG1262 3.9 28.6 1.0 C A:SER1261 4.0 24.2 1.0 NH2 A:ARG1259 4.1 39.6 1.0 CZ A:PHE992 4.1 24.3 1.0 NH2 A:ARG1262 4.2 28.6 1.0 CG A:ARG1262 4.2 26.8 1.0 CZ A:ARG1259 4.3 38.9 1.0 CB A:ARG1262 4.4 25.8 1.0 NE A:ARG1262 4.4 28.3 1.0 CA A:ARG1262 4.5 24.9 0.5 CE1 A:PHE992 4.8 24.6 1.0 N A:SER1261 4.8 23.9 1.0 O A:ALA1260 4.8 21.6 1.0 OG A:SER1261 4.9 24.2 1.0 CD A:ARG1262 4.9 27.8 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form


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 Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2012 b:43.5 occ:1.00 N B:ARG1262 3.5 29.9 1.0 NH1 B:ARG1259 3.5 47.8 1.0 O B:HOH2178 3.6 35.9 1.0 CZ B:ARG1262 3.7 29.7 1.0 O B:HOH2171 3.7 37.2 1.0 NH1 B:ARG1262 3.7 28.5 1.0 CA B:SER1261 3.8 31.2 1.0 NH2 B:ARG1262 3.8 29.4 1.0 CZ B:PHE992 3.8 36.1 1.0 NH2 B:ARG1259 4.0 45.1 1.0 CB B:SER1261 4.0 31.4 1.0 C B:SER1261 4.1 30.8 1.0 CG B:ARG1262 4.1 30.0 1.0 NE B:ARG1262 4.1 29.8 1.0 CZ B:ARG1259 4.2 44.4 1.0 CB B:ARG1262 4.3 29.9 1.0 CA B:ARG1262 4.5 29.5 0.5 CE1 B:PHE992 4.6 36.4 1.0 CD B:ARG1262 4.8 30.2 1.0 CE2 B:PHE992 4.8 36.0 1.0 O B:ALA1260 4.9 33.4 1.0 N B:SER1261 5.0 32.3 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Carbamoyl Phosphate Synthetase I (CPS1), Ligand-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl2012 b:26.3 occ:1.00 O D:HOH2290 3.2 47.0 1.0 N D:ARG1262 3.3 25.7 1.0 CA D:SER1261 3.5 24.4 1.0 NH1 D:ARG1259 3.5 39.3 1.0 CB D:SER1261 3.6 24.6 1.0 NH1 D:ARG1262 3.9 30.9 1.0 C D:SER1261 3.9 24.8 1.0 CZ D:ARG1262 3.9 31.2 1.0 CZ D:PHE992 4.0 22.3 1.0 NH2 D:ARG1259 4.1 38.5 1.0 NH2 D:ARG1262 4.2 30.4 1.0 CG D:ARG1262 4.2 28.7 1.0 CB D:ARG1262 4.3 26.3 1.0 CZ D:ARG1259 4.3 35.8 1.0 CA D:ARG1262 4.4 25.2 0.5 NE D:ARG1262 4.4 30.7 1.0 CE1 D:PHE992 4.7 23.0 1.0 O D:HOH2308 4.7 27.0 1.0 N D:SER1261 4.7 24.1 1.0 O D:ALA1260 4.7 22.9 1.0 OG D:SER1261 4.8 24.7 1.0 CD D:ARG1262 4.9 29.2 1.0 O D:HOH2106 4.9 31.6 1.0

S.De Cima, L.M.Polo, C.Diez-Fernandez, A.I.Martinez, J.Cervera, I.Fita, V.Rubio. Structure of Human Carbamoyl Phosphate Synthetase: Deciphering the on/Off Switch of Human Ureagenesis. Sci Rep V. 5 16950 2015.
ISSN: ESSN 2045-2322
PubMed: 26592762
DOI: 10.1038/SREP16950