Magnesium in PDB 5fm0: Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative)

All present enzymatic activity of Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative):
6.2.1.14;

The structure of Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative), PDB code: 5fm0 was solved by L.Moynie, M.Wang, D.J.Campopiano, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.35 / 2.44
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.610, 78.360, 166.700, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.2

The structure of Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative) also contains other interesting chemical elements:

Platinum

(Pt)

6 atoms

The binding sites of Magnesium atom in the Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative) (pdb code 5fm0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative), PDB code: 5fm0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1258 b:61.9 occ:1.00 O12 A:PPV1257 2.1 63.8 1.0 O A:HOH2006 2.3 49.9 1.0 O A:HOH2005 2.3 60.6 1.0 O21 A:PPV1257 2.4 50.7 1.0 OAH A:WAQ1256 2.4 44.1 1.0 O A:HOH2010 3.4 50.2 1.0 OE1 A:GLU173 3.5 68.0 1.0 P2 A:PPV1257 3.6 59.9 1.0 P1 A:PPV1257 3.7 54.0 1.0 PBG A:WAQ1256 3.8 45.5 1.0 OPP A:PPV1257 4.1 73.8 1.0 NZ A:LYS49 4.1 67.2 1.0 O A:GLY29 4.3 63.5 1.0 OAU A:WAQ1256 4.3 66.3 1.0 O32 A:PPV1257 4.4 81.5 1.0 O31 A:PPV1257 4.4 53.7 1.0 CD A:GLU173 4.6 58.0 1.0 N7 A:WAQ1256 4.6 49.2 1.0 CB A:GLU173 4.6 37.9 1.0 O22 A:PPV1257 4.6 66.8 1.0 C8 A:WAQ1256 4.7 51.1 1.0 O5' A:WAQ1256 4.7 41.9 1.0 NH2 A:ARG145 4.7 47.8 1.0 OE2 A:GLU31 4.9 72.2 1.0 O11 A:PPV1257 5.0 56.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the 6-Carboxyhexanoate-Coa Ligase (Biow)From Bacillus Subtilis (PTCL4 Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1259 b:60.8 occ:1.00 O32 A:PPV1257 2.1 81.5 1.0 OD1 A:ASP195 2.2 57.1 1.0 O A:HOH2004 2.3 49.8 1.0 OAD A:WAQ1256 2.4 51.8 1.0 OD1 A:ASP196 2.4 70.3 1.0 O31 A:PPV1257 2.6 53.7 1.0 OPP A:PPV1257 3.2 73.8 1.0 CG A:ASP195 3.3 51.8 1.0 P2 A:PPV1257 3.3 59.9 1.0 PBG A:WAQ1256 3.3 45.5 1.0 CG A:ASP196 3.3 68.8 1.0 OAH A:WAQ1256 3.5 44.1 1.0 P1 A:PPV1257 3.5 54.0 1.0 OD2 A:ASP196 3.6 69.5 1.0 OD2 A:ASP195 3.6 62.7 1.0 NE2 A:HIS53 3.9 58.1 1.0 CE1 A:HIS53 4.0 64.1 1.0 O5' A:WAQ1256 4.1 41.9 1.0 O12 A:PPV1257 4.1 63.8 1.0 C5' A:WAQ1256 4.1 41.0 1.0 OG A:SER194 4.3 55.6 1.0 N A:ASP196 4.4 44.4 1.0 O22 A:PPV1257 4.4 66.8 1.0 N A:ASP195 4.4 47.9 1.0 O21 A:PPV1257 4.4 50.7 1.0 CB A:ASP195 4.6 53.1 1.0 CD A:ARG55 4.6 57.7 1.0 O11 A:PPV1257 4.6 56.0 1.0 O A:ILE27 4.7 61.9 1.0 CB A:ASP196 4.7 53.7 1.0 C A:ASP195 4.8 43.6 1.0 OAU A:WAQ1256 4.8 66.3 1.0 CA A:ASP195 4.8 47.9 1.0 O3' A:WAQ1256 4.8 47.1 1.0 C3' A:WAQ1256 4.9 48.9 1.0

M.Wang, L.Moynie, P.J.Harrison, V.Kelly, A.Piper, J.H.Naismith, D.J.Campopiano. Using the Pimeloyl-Coa Synthetase Adenylation Fold to Synthesize Fatty Acid Thioesters. Nat. Chem. Biol. V. 13 660 2017.
ISSN: ESSN 1552-4469
PubMed: 28414710
DOI: 10.1038/NCHEMBIO.2361