Magnesium in PDB 3kki: Plp-Dependent Acyl-Coa Transferase Cqsa

The structure of Plp-Dependent Acyl-Coa Transferase Cqsa, PDB code: 3kki was solved by R.C.Kelly, P.D.Jeffrey, F.M.Hughson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.81 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.621, 177.443, 70.677, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.4

The binding sites of Magnesium atom in the Plp-Dependent Acyl-Coa Transferase Cqsa (pdb code 3kki). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Plp-Dependent Acyl-Coa Transferase Cqsa, PDB code: 3kki:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Plp-Dependent Acyl-Coa Transferase Cqsa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Plp-Dependent Acyl-Coa Transferase Cqsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg391 b:37.1 occ:1.00 O A:HOH449 2.6 50.3 1.0 O3 A:PLP390 2.7 21.0 0.6 NH1 A:ARG358 3.3 20.4 1.0 C4A A:PLP390 3.4 21.8 0.6 NE2 A:HIS205 3.8 18.5 1.0 C3 A:PLP390 3.9 20.6 0.6 O4A A:PLP390 3.9 23.1 0.6 CE1 A:HIS205 3.9 19.6 1.0 CB A:SER177 4.0 16.3 1.0 O B:HOH546 4.1 45.9 1.0 NZ A:LYS236 4.1 30.6 1.0 NH2 A:ARG358 4.1 21.2 1.0 C4 A:PLP390 4.2 21.0 0.6 CZ A:ARG358 4.2 20.3 1.0 O A:HOH490 4.3 26.0 1.0 O A:HOH461 4.4 57.0 1.0 NE2 A:HIS133 4.5 23.3 1.0 CE A:LYS236 4.5 24.0 1.0 OD1 A:ASN47 4.6 26.3 1.0 ND2 A:ASN47 4.6 22.2 1.0 CZ A:PHE345 4.6 19.6 1.0 OG A:SER177 4.6 21.0 1.0 CD2 A:HIS133 4.7 24.1 1.0 CE1 A:PHE345 4.9 20.3 1.0 O B:HOH460 4.9 30.1 1.0 CG A:ASN47 4.9 21.6 1.0

Magnesium binding site 2 out of 2 in the Plp-Dependent Acyl-Coa Transferase Cqsa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Plp-Dependent Acyl-Coa Transferase Cqsa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg391 b:46.9 occ:1.00 O3 B:PLP390 2.6 23.8 0.6 C4A B:PLP390 3.5 24.9 0.6 NH1 B:ARG358 3.5 28.4 1.0 O4A B:PLP390 3.5 26.1 0.6 NE2 B:HIS205 3.6 27.8 1.0 CE1 B:HIS205 3.7 25.0 1.0 C3 B:PLP390 3.8 23.8 0.6 CB B:SER177 3.9 27.4 1.0 NZ B:LYS236 3.9 33.5 1.0 C4 B:PLP390 4.1 23.7 0.6 CE B:LYS236 4.2 25.9 1.0 NH2 B:ARG358 4.3 32.2 1.0 CZ B:ARG358 4.4 31.2 1.0 O B:HOH470 4.4 31.1 1.0 NE2 B:HIS133 4.4 25.1 1.0 OD1 B:ASN47 4.6 30.3 1.0 O B:HOH476 4.6 59.4 1.0 OG B:SER177 4.6 31.0 1.0 CD2 B:HIS133 4.6 25.8 1.0 ND2 B:ASN47 4.7 31.8 1.0 CZ B:PHE345 4.8 31.5 1.0 CD2 B:HIS205 4.9 24.5 1.0 CA B:SER177 4.9 24.6 1.0 CG B:ASN47 4.9 30.6 1.0 C2 B:PLP390 5.0 23.2 0.6

R.C.Kelly, M.E.Bolitho, D.A.Higgins, W.Lu, W.L.Ng, P.D.Jeffrey, J.D.Rabinowitz, M.F.Semmelhack, F.M.Hughson, B.L.Bassler. The Vibrio Cholerae Quorum-Sensing Autoinducer Cai-1: Analysis of the Biosynthetic Enzyme Cqsa. Nat.Chem.Biol. V. 5 891 2009.
ISSN: ISSN 1552-4450
PubMed: 19838203
DOI: 10.1038/NCHEMBIO.237