Magnesium in PDB 5z45: Crystal Structure of Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile

The structure of Crystal Structure of Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile, PDB code: 5z45 was solved by T.Awakawa, Y.Nakashima, T.Mori, I.Abe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.20 / 2.60
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	116.257, 116.257, 49.687, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 27.1

The binding sites of Magnesium atom in the Crystal Structure of Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile (pdb code 5z45). 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 Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile, PDB code: 5z45:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile


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 Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:77.7 occ:1.00 OD2 A:ASP65 1.8 0.8 1.0 OE2 A:GLU63 2.0 94.1 1.0 OD1 A:ASN41 2.1 94.3 1.0 CG A:ASP65 2.7 91.8 1.0 CD A:GLU63 3.0 77.6 1.0 CG A:ASN41 3.2 60.6 1.0 OD1 A:ASP65 3.5 76.9 1.0 OE1 A:GLU63 3.5 84.2 1.0 CB A:ASP65 3.6 80.9 1.0 ND2 A:ASN41 3.8 48.5 1.0 N A:ASP65 3.9 71.5 1.0 O A:ASP40 4.2 57.8 1.0 CG A:GLU63 4.3 66.0 1.0 O A:HOH510 4.3 49.4 1.0 N A:GLU64 4.3 71.8 1.0 CB A:ASN41 4.3 68.9 1.0 CA A:ASP65 4.4 70.7 1.0 CA A:GLU63 4.5 52.4 1.0 CA A:ASN41 4.7 63.1 1.0 CB A:GLU63 4.8 59.7 1.0 C A:GLU63 4.9 61.6 1.0 C A:GLU64 4.9 74.5 1.0 C A:ASP40 5.0 61.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile


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 Prenyltransferase AMBP1 PH6.5 Complexed with Gspp and Cis-Indolyl Vinyl Isonitrile within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:96.8 occ:1.00 OD2 B:ASP65 1.7 0.6 1.0 OD1 B:ASN41 1.9 0.6 1.0 OE1 B:GLU63 2.3 64.5 1.0 CG B:ASP65 2.8 88.9 1.0 CG B:ASN41 3.1 59.2 1.0 CD B:GLU63 3.3 69.8 1.0 OD1 B:ASP65 3.6 98.2 1.0 OE2 B:GLU63 3.6 78.2 1.0 CB B:ASP65 3.7 60.9 1.0 N B:ASP65 3.8 55.0 1.0 ND2 B:ASN41 4.0 52.9 1.0 N B:GLU64 4.1 58.2 1.0 CB B:ASN41 4.2 46.3 1.0 O B:ASP40 4.3 81.4 1.0 CA B:ASN41 4.4 48.9 1.0 CA B:ASP65 4.4 61.1 1.0 CG B:GLU63 4.6 62.9 1.0 CA B:GLU63 4.6 53.4 1.0 C B:GLU64 4.8 54.5 1.0 C B:GLU63 4.9 61.4 1.0 C B:ASP40 4.9 87.8 1.0 CA B:GLU64 5.0 51.1 1.0

T.Awakawa, T.Mori, Y.Nakashima, R.Zhai, C.P.Wong, M.L.Hillwig, X.Liu, I.Abe. Molecular Insight Into the MG2+-Dependent Allosteric Control of Indole Prenylation By Aromatic Prenyltransferase AMBP1 Angew. Chem. Int. Ed. Engl. V. 57 6810 2018.
ISSN: ESSN 1521-3773
PubMed: 29677386
DOI: 10.1002/ANIE.201800855