Magnesium in PDB 6ksa: Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA

All present enzymatic activity of Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA:
1.3.8.1;

The structure of Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA, PDB code: 6ksa was solved by X.Liu, X.B.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.68 / 1.77
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.934, 206.586, 74.064, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 17.1

The binding sites of Magnesium atom in the Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA (pdb code 6ksa). 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 E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA, PDB code: 6ksa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA


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 E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg704 b:32.9 occ:1.00 O A:HIS385 2.6 26.2 1.0 OH A:TYR472 2.8 22.9 1.0 O A:HOH1158 2.8 42.8 1.0 O4 A:SO4703 3.0 33.4 1.0 OE1 A:GLU476 3.1 27.1 1.0 HB3 A:HIS385 3.2 29.9 1.0 HA A:HIS385 3.2 31.1 1.0 HH A:TYR472 3.3 27.6 1.0 HE1 A:TYR472 3.3 26.6 1.0 CD A:GLU476 3.5 31.1 1.0 C A:HIS385 3.5 26.9 1.0 CA A:HIS385 3.7 25.9 1.0 CZ A:TYR472 3.8 24.6 1.0 OE2 A:GLU476 3.8 27.3 1.0 CB A:HIS385 3.9 24.9 1.0 S A:SO4703 3.9 67.3 1.0 HD1 A:HIS385 3.9 31.4 1.0 CE1 A:TYR472 3.9 22.2 1.0 HG13 A:VAL387 4.0 39.8 1.0 O A:HOH1219 4.0 50.9 1.0 O1 A:SO4703 4.1 34.2 1.0 HG3 A:GLU476 4.1 27.1 1.0 O2 A:SO4703 4.1 29.9 1.0 O A:HOH801 4.3 42.8 1.0 HG12 A:VAL387 4.4 39.8 1.0 CG A:GLU476 4.4 22.5 1.0 ND1 A:HIS385 4.5 26.2 1.0 CG1 A:VAL387 4.6 33.2 1.0 HB2 A:HIS385 4.6 29.9 1.0 HG11 A:VAL387 4.7 39.8 1.0 CG A:HIS385 4.7 24.5 1.0 N A:GLY386 4.8 27.6 1.0 HG2 A:GLU476 4.9 27.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA


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 E447A Acyl-Coa Dehydrogenase FADE5 Mutant From Mycobacteria Smegmatis in Complex with C18COA within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg705 b:31.8 occ:1.00 O B:HIS385 2.5 23.8 1.0 OH B:TYR472 2.8 21.3 1.0 O1 B:SO4703 2.9 36.6 1.0 O B:HOH1072 3.0 49.0 1.0 HB3 B:HIS385 3.2 29.7 1.0 O B:HOH1040 3.2 52.1 1.0 HA B:HIS385 3.2 32.8 1.0 OE1 B:GLU476 3.3 28.1 1.0 HH B:TYR472 3.3 25.6 1.0 HE1 B:TYR472 3.3 25.5 1.0 C B:HIS385 3.5 26.4 1.0 CD B:GLU476 3.6 27.4 1.0 CA B:HIS385 3.7 27.3 1.0 CZ B:TYR472 3.8 24.9 1.0 OE2 B:GLU476 3.8 28.1 1.0 S B:SO4703 3.8 72.5 1.0 CB B:HIS385 3.9 24.7 1.0 HD1 B:HIS385 3.9 32.5 1.0 CE1 B:TYR472 3.9 21.2 1.0 HG13 B:VAL387 3.9 35.1 1.0 O3 B:SO4703 4.1 28.7 1.0 O2 B:SO4703 4.1 30.9 1.0 HG3 B:GLU476 4.2 29.3 1.0 HG12 B:VAL387 4.3 35.1 1.0 ND1 B:HIS385 4.5 27.1 1.0 CG1 B:VAL387 4.5 29.2 1.0 CG B:GLU476 4.5 24.4 1.0 HG11 B:VAL387 4.6 35.1 1.0 HB2 B:HIS385 4.6 29.7 1.0 CG B:HIS385 4.6 20.6 1.0 N B:GLY386 4.7 24.8 1.0 HG2 B:GLU476 4.9 29.3 1.0 HA3 B:GLY386 5.0 29.1 1.0

X.Chen, J.Chen, B.Yan, W.Zhang, L.W.Guddat, X.Liu, Z.Rao. Structural Basis For the Broad Substrate Specificity of Two Acyl-Coa Dehydrogenases FADE5 From Mycobacteria. Proc.Natl.Acad.Sci.Usa V. 117 16324 2020.
ISSN: ESSN 1091-6490
PubMed: 32601219
DOI: 10.1073/PNAS.2002835117