Chlorine in PDB 5trc: Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase

All present enzymatic activity of Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase:
6.3.4.14; 6.4.1.2;

The structure of Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase, PDB code: 5trc was solved by J.Wei, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.57 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.433, 93.191, 110.944, 90.00, 99.57, 90.00
R / Rfree (%)	22.3 / 28.7

The binding sites of Chlorine atom in the Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase (pdb code 5trc). 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 Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase, PDB code: 5trc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase


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 Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1601 b:71.6 occ:1.00 NH1 A:ARG1108 2.6 68.7 1.0 N A:PHE1083 3.4 61.8 1.0 N A:VAL1082 3.5 64.3 1.0 CG A:PHE1083 3.5 55.4 1.0 CB A:PHE1083 3.6 59.2 1.0 CD2 A:PHE1083 3.8 57.7 1.0 CD1 A:PHE1083 3.9 59.9 1.0 CZ A:ARG1108 3.9 59.3 1.0 OH A:TYR1272 3.9 76.7 1.0 CG1 A:VAL1081 4.0 58.5 1.0 CA A:PHE1083 4.1 64.0 1.0 CA A:VAL1082 4.3 68.7 1.0 C A:VAL1082 4.3 65.1 1.0 CA A:VAL1081 4.4 68.3 1.0 CE1 A:TYR1272 4.4 56.5 1.0 C A:VAL1081 4.4 68.3 1.0 CE2 A:PHE1083 4.4 63.0 1.0 CE1 A:PHE1083 4.5 63.0 1.0 CB A:VAL1082 4.5 64.9 1.0 CD A:ARG1108 4.6 59.6 1.0 NE A:ARG1108 4.7 59.4 1.0 CZ A:TYR1272 4.7 62.9 1.0 NH2 A:ARG1108 4.7 68.2 1.0 CZ A:PHE1083 4.8 62.4 1.0 CB A:VAL1081 4.9 59.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase


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 Phosphorylated AC3-AC5 Domains of Yeast Acetyl- Coa Carboxylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1601 b:76.3 occ:1.00 NH1 B:ARG1108 2.7 76.3 1.0 OH B:TYR1272 3.2 57.6 1.0 CG B:PHE1083 3.4 72.7 1.0 N B:PHE1083 3.5 70.3 1.0 CB B:PHE1083 3.7 71.5 1.0 CD2 B:PHE1083 3.7 77.9 1.0 N B:VAL1082 3.8 84.6 1.0 CD1 B:PHE1083 3.8 77.5 1.0 CZ B:ARG1108 4.0 86.2 1.0 CE1 B:TYR1272 4.1 64.3 1.0 CZ B:TYR1272 4.2 58.5 1.0 CA B:PHE1083 4.2 69.9 1.0 CE2 B:PHE1083 4.3 76.5 1.0 CE1 B:PHE1083 4.3 79.1 1.0 C B:VAL1082 4.5 77.1 1.0 NH1 B:ARG1343 4.5 69.6 1.0 CA B:VAL1082 4.5 81.4 1.0 CZ B:PHE1083 4.5 76.0 1.0 CA B:VAL1081 4.6 72.2 1.0 CG2 B:VAL1081 4.6 78.0 1.0 C B:VAL1081 4.7 84.1 1.0 NH2 B:ARG1108 4.7 86.2 1.0 CB B:VAL1082 4.7 85.3 1.0 CB B:VAL1081 4.9 74.8 1.0 NE B:ARG1108 5.0 93.9 1.0

J.Wei, Y.Zhang, T.Y.Yu, K.Sadre-Bazzaz, M.J.Rudolph, G.A.Amodeo, L.S.Symington, T.Walz, L.Tong. A Unified Molecular Mechanism For the Regulation of Acetyl-Coa Carboxylase By Phosphorylation. Cell Discov V. 2 16044 2016.
ISSN: ESSN 2056-5968
PubMed: 27990296
DOI: 10.1038/CELLDISC.2016.44