Arsenic in PDB 5yge: Arga Complexed with Acecoa and Glutamate

All present enzymatic activity of Arga Complexed with Acecoa and Glutamate:
2.3.1.1;

The structure of Arga Complexed with Acecoa and Glutamate, PDB code: 5yge was solved by X.Yang, L.Wu, Y.Ran, A.Xu, B.Zhang, X.Yang, R.Zhang, Z.Rao, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.17 / 2.04
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.728, 73.728, 187.231, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.1

The binding sites of Arsenic atom in the Arga Complexed with Acecoa and Glutamate (pdb code 5yge). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the Arga Complexed with Acecoa and Glutamate, PDB code: 5yge:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in the Arga Complexed with Acecoa and Glutamate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Arga Complexed with Acecoa and Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ A:As203 b:94.3 occ:0.67 AS A:CAD203 0.0 94.3 0.7 O1 A:CAD203 1.6 31.9 1.0 C1 A:CAD203 1.9 61.0 1.0 C2 A:CAD203 1.9 71.5 1.0 SG A:CYS8 2.2 91.3 1.0 CB A:CYS8 2.6 45.0 1.0 CA A:CYS8 3.5 44.9 1.0 N A:CYS8 4.2 43.0 1.0 CD A:PRO56 4.2 30.6 1.0 CG A:PRO56 4.3 37.2 1.0 O A:ASP7 4.6 33.5 1.0 CE A:MET87 4.6 30.4 1.0 C A:ASP7 4.6 39.3 1.0 C A:CYS8 4.7 44.5 1.0 CB A:HIS90 4.9 21.4 1.0

Arsenic binding site 2 out of 4 in the Arga Complexed with Acecoa and Glutamate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Arga Complexed with Acecoa and Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ A:As204 b:44.3 occ:0.64 AS A:CAD204 0.0 44.3 0.6 O1 A:CAD204 1.7 76.9 1.0 C1 A:CAD204 1.9 56.5 1.0 C2 A:CAD204 2.1 32.7 1.0 SG A:CYS144 2.1 40.2 1.0 CB A:CYS144 2.9 38.5 1.0 O A:HOH345 3.1 39.1 1.0 CA A:CYS144 3.8 36.0 1.0 CZ A:PHE140 4.3 26.3 1.0 OE2 B:GLU45 4.3 49.8 1.0 CE2 A:PHE140 4.3 23.6 1.0 CD1 A:LEU157 4.4 25.6 1.0 O A:HOH374 4.7 43.3 1.0 N A:CYS144 4.7 30.0 1.0 CD2 A:LEU157 4.9 25.5 1.0 C A:CYS144 4.9 30.5 1.0 CG2 B:VAL41 5.0 19.6 1.0

Arsenic binding site 3 out of 4 in the Arga Complexed with Acecoa and Glutamate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Arga Complexed with Acecoa and Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ B:As203 b:80.2 occ:0.60 AS B:CAD203 0.0 80.2 0.6 O1 B:CAD203 1.7 0.2 1.0 SG B:CYS8 1.8 75.6 1.0 C2 B:CAD203 1.9 43.7 1.0 C1 B:CAD203 1.9 69.8 1.0 CB B:CYS8 3.2 82.6 1.0 CA B:CYS8 3.9 80.8 1.0 CE B:MET87 4.2 20.6 1.0 CD1 B:ILE92 4.5 20.6 1.0 C B:CYS8 4.6 80.9 1.0 NE2 B:HIS55 4.6 39.8 1.0 CE1 B:HIS55 4.6 38.1 1.0 N B:ARG9 4.6 76.4 1.0 CG1 B:ILE92 4.7 23.3 1.0 CD2 B:HIS55 4.8 36.1 1.0 ND1 B:HIS55 4.8 33.5 1.0 CB B:HIS90 4.8 39.9 1.0 CD B:PRO56 4.9 20.7 1.0 CG B:HIS55 4.9 28.2 1.0

Arsenic binding site 4 out of 4 in the Arga Complexed with Acecoa and Glutamate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Arga Complexed with Acecoa and Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ B:As204 b:30.6 occ:0.69 AS B:CAD204 0.0 30.6 0.7 O1 B:CAD204 1.7 54.4 1.0 C2 B:CAD204 2.0 0.0 1.0 C1 B:CAD204 2.0 27.1 1.0 SG B:CYS144 2.2 31.0 1.0 CB B:CYS144 3.0 29.0 1.0 O A:HOH317 3.3 27.2 1.0 CA B:CYS144 3.8 22.8 1.0 O B:HOH371 3.8 32.2 1.0 CZ B:PHE140 4.0 23.7 1.0 CE2 B:PHE140 4.2 21.8 1.0 CD1 B:LEU157 4.4 18.0 1.0 OE2 A:GLU45 4.4 41.5 1.0 N B:CYS144 4.7 21.2 1.0 CD2 B:LEU157 4.7 15.5 1.0 O B:HOH389 4.7 29.0 1.0 CE1 B:PHE140 4.7 25.8 1.0 C B:CYS144 4.9 20.2 1.0

X.Yang, L.Wu, Y.Ran, A.Xu, B.Zhang, X.Yang, R.Zhang, Z.Rao, J.Li. Crystal Structure of L-Glutamate N-Acetyltransferase Arga From Mycobacterium Tuberculosis Biochim. Biophys. Acta V.1865 1800 2017.
ISSN: ISSN 0006-3002
PubMed: 28943401
DOI: 10.1016/J.BBAPAP.2017.09.009