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Magnesium in PDB 6wyi: Crystal Structure of ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis

Protein crystallography data

The structure of Crystal Structure of ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis, PDB code: 6wyi was solved by A.C.Bonds, M.Garcia-Diaz, N.S.Sampson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.71 / 1.92
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 75.413, 75.413, 68.890, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 23.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis (pdb code 6wyi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis, PDB code: 6wyi:

Magnesium binding site 1 out of 1 in 6wyi

Go back to Magnesium Binding Sites List in 6wyi
Magnesium binding site 1 out of 1 in the Crystal Structure of ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis


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 ECHA19, Enoyl-Coa Hydratase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:38.8
occ:0.33
O A:HOH475 2.1 37.7 1.0
O A:HOH428 2.2 36.7 1.0
O A:HOH467 4.2 49.1 1.0
O A:HOH451 4.3 42.3 1.0
O A:HOH469 4.5 38.2 1.0
O A:ARG154 4.5 35.1 1.0
CA A:ARG154 4.9 32.0 1.0

Reference:

A.C.Bonds, T.Yuan, J.M.Werman, J.Jang, R.Lu, N.M.Nesbitt, M.Garcia-Diaz, N.S.Sampson. Post-Translational Succinylation Ofmycobacterium Tuberculosisenoyl-Coa Hydratase ECHA19 Slows Catalytic Hydration of Cholesterol Catabolite 3-Oxo-Chol-4,22-Diene-24-Oyl-Coa. Acs Infect Dis. V. 6 2214 2020.
ISSN: ESSN 2373-8227
PubMed: 32649175
DOI: 10.1021/ACSINFECDIS.0C00329
Page generated: Tue Oct 1 23:19:46 2024

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