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Manganese in PDB 8a78: PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp

Enzymatic activity of PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp

All present enzymatic activity of PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp:
2.5.1.1;

Protein crystallography data

The structure of PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp, PDB code: 8a78 was solved by F.Ecker, W.Boland, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.09, 78.79, 88.48, 90, 102.17, 90
R / Rfree (%) 14.8 / 18.9

Other elements in 8a78:

The structure of PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp (pdb code 8a78). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp, PDB code: 8a78:

Manganese binding site 1 out of 1 in 8a78

Go back to Manganese Binding Sites List in 8a78
Manganese binding site 1 out of 1 in the PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of PCIDS1_F315A in Complex with MG2+/MN2+ and Gpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:25.6
occ:1.00
OD1 A:ASP179 2.1 20.3 1.0
O A:HOH719 2.1 24.3 1.0
O A:HOH631 2.2 21.3 1.0
OD2 A:ASP183 2.2 22.2 1.0
O A:HOH645 2.2 22.6 1.0
O1A A:GPP505 2.2 21.0 1.0
CG A:ASP183 3.0 22.2 1.0
CG A:ASP179 3.1 21.6 1.0
OD1 A:ASP183 3.1 24.9 1.0
MG A:MG502 3.2 16.7 1.0
PA A:GPP505 3.3 23.4 1.0
OD2 A:ASP179 3.4 20.6 1.0
O2A A:GPP505 3.9 27.3 1.0
O1 A:GPP505 3.9 24.9 1.0
NE2 A:GLN247 4.0 20.1 1.0
O A:HOH612 4.0 33.8 1.0
OE1 A:GLN247 4.1 22.0 1.0
C1 A:GPP505 4.3 26.0 1.0
O A:HOH615 4.3 23.8 1.0
OD2 A:ASP250 4.3 27.0 1.0
O A:HOH608 4.4 42.0 1.0
CB A:ASP183 4.4 22.7 1.0
CB A:ASP179 4.4 19.9 1.0
CD A:GLN247 4.5 20.7 1.0
O A:HOH708 4.5 27.4 1.0
C2 A:GPP505 4.5 26.6 1.0
O1B A:GPP505 4.7 27.4 1.0
O A:ASP179 4.7 21.9 1.0
O3A A:GPP505 4.7 27.0 1.0
O A:HOH648 4.9 22.6 1.0
CA A:ASP179 5.0 19.4 1.0

Reference:

F.Ecker, W.Boland, M.Groll. Metal-Dependent Enzyme Symmetry Guides the Biosynthetic Flux of Terpene Precursors To Be Published 2023.
DOI: 10.1038/S41557-023-01235-9
Page generated: Sun Oct 6 11:17:18 2024

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