Magnesium in PDB 4w82: Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase

All present enzymatic activity of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase:
1.3.1.39;

The structure of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase, PDB code: 4w82 was solved by K.H.Sippel, N.K.Vyas, B.Sankaran, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.27 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.310, 59.040, 61.430, 94.96, 101.11, 95.09
R / Rfree (%)	18.7 / 21.7

The structure of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase (pdb code 4w82). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase, PDB code: 4w82:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1902 b:27.3 occ:1.00 O A:HOH2017 2.0 32.1 1.0 O A:HOH2004 2.0 46.1 1.0 O A:HOH2037 2.0 49.8 1.0 O A:HOH2075 2.1 21.2 1.0 NZ A:LYS1827 2.1 20.5 1.0 CE A:LYS1827 2.9 21.4 1.0 OE1 A:GLU1644 3.8 23.7 1.0 CD A:LYS1827 4.3 25.8 1.0 O A:LEU1826 4.3 19.6 1.0 O A:HOH2025 4.3 27.1 1.0 O A:HOH2046 4.5 53.0 1.0 CA A:LYS1827 4.7 19.5 1.0 O A:PRO1825 4.8 16.7 1.0 CG A:LYS1827 4.8 21.6 1.0 C A:LEU1826 4.8 20.1 1.0 N A:LYS1827 4.9 19.5 1.0

Magnesium binding site 2 out of 2 in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1901 b:30.2 occ:1.00 O B:HOH2008 1.9 30.0 1.0 NZ B:LYS1827 2.0 21.3 1.0 O B:HOH2055 2.0 22.7 1.0 O B:HOH2015 2.0 35.2 1.0 O B:HOH2036 2.3 33.3 1.0 CE B:LYS1827 2.9 21.1 1.0 OE1 B:GLU1644 3.8 30.4 1.0 O B:HOH2024 4.1 29.1 1.0 CD B:LYS1827 4.2 26.4 1.0 O B:LEU1826 4.2 19.4 1.0 CA B:LYS1827 4.6 17.4 1.0 O B:HOH2039 4.6 62.1 1.0 CG B:LYS1827 4.7 22.4 1.0 C B:LEU1826 4.8 18.1 1.0 N B:LYS1827 4.8 17.5 1.0 O B:PRO1825 4.9 15.4 1.0

K.H.Sippel, N.K.Vyas, W.Zhang, B.Sankaran, F.A.Quiocho. Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition. J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
PubMed: 25301948
DOI: 10.1074/JBC.M114.608547