Magnesium in PDB 6vl1: Crystal Structure of the N-Prenyltransferase Daba in Complex with Ngg and MG2+

The structure of Crystal Structure of the N-Prenyltransferase Daba in Complex with Ngg and MG2+, PDB code: 6vl1 was solved by J.R.Chekan, J.P.Noel, B.S.Moore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.71 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	123.425, 123.425, 113.208, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 19.5

The binding sites of Magnesium atom in the Crystal Structure of the N-Prenyltransferase Daba in Complex with Ngg and MG2+ (pdb code 6vl1). 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 the N-Prenyltransferase Daba in Complex with Ngg and MG2+, PDB code: 6vl1:

Magnesium binding site 1 out of 1 in the Crystal Structure of the N-Prenyltransferase Daba in Complex with Ngg and MG2+


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 N-Prenyltransferase Daba in Complex with Ngg and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:64.2 occ:1.00 O A:HOH801 2.1 57.8 1.0 O A:HOH723 2.2 55.4 1.0 OE2 A:GLU359 2.4 68.0 1.0 O A:HOH736 2.4 36.5 1.0 O13 A:R1V602 2.5 76.6 1.0 OE1 A:GLU359 2.6 58.8 1.0 CD A:GLU359 2.9 58.8 1.0 O A:PHE366 3.2 40.4 1.0 C11 A:R1V602 3.4 70.8 1.0 OD1 A:ASP352 3.7 26.8 1.0 O A:HOH948 3.9 39.8 1.0 O A:HOH964 3.9 34.9 1.0 O12 A:R1V602 4.0 55.7 1.0 OD2 A:ASP364 4.1 62.7 1.0 C10 A:R1V602 4.2 65.7 1.0 ND2 A:ASN367 4.2 24.1 1.0 CB A:ASN367 4.3 27.1 1.0 C A:PHE366 4.3 44.7 1.0 OG1 A:THR355 4.3 25.4 1.0 CG A:GLU359 4.4 43.9 1.0 OH A:TYR302 4.4 30.6 1.0 C14 A:R1V602 4.5 45.4 1.0 CA A:ASN367 4.5 30.2 1.0 CG A:ASN367 4.7 35.4 1.0 OD1 A:ASN351 4.7 28.0 1.0 CG A:ASP352 4.8 26.8 1.0 N A:ASN367 4.8 30.5 1.0 O A:HOH889 4.9 55.6 1.0

J.R.Chekan, S.M.K.Mckinnie, J.P.Noel, B.S.Moore. Algal Neurotoxin Biosynthesis Repurposes the Terpene Cyclase Structural Fold Into An N-Prenyltransferase To Be Published.