Magnesium in PDB 3n45: Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+

All present enzymatic activity of Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+:
2.5.1.1; 2.5.1.10;

The structure of Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+, PDB code: 3n45 was solved by J.-M.Rondeau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.03 / 1.88
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.753, 110.753, 67.966, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+ (pdb code 3n45). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+, PDB code: 3n45:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg355 b:39.2 occ:1.00 O15 F:ZOL354 1.9 38.9 1.0 OD1 F:ASP103 2.0 38.9 1.0 O F:HOH361 2.1 36.1 1.0 O F:HOH358 2.1 37.1 1.0 O11 F:ZOL354 2.1 39.2 1.0 OD2 F:ASP107 2.2 37.7 1.0 CG F:ASP103 3.1 40.6 1.0 MG F:MG3 3.2 40.3 1.0 P14 F:ZOL354 3.2 42.0 1.0 CG F:ASP107 3.2 37.0 1.0 P9 F:ZOL354 3.3 38.4 1.0 OD2 F:ASP103 3.5 39.2 1.0 CB F:ASP107 3.7 37.5 1.0 C8 F:ZOL354 3.8 39.5 1.0 O F:HOH373 3.8 40.5 1.0 O12 F:ZOL354 4.0 38.9 1.0 O17 F:ZOL354 4.0 37.2 1.0 C7 F:ZOL354 4.0 39.9 1.0 NH2 F:ARG112 4.1 40.3 1.0 O F:HOH364 4.2 36.8 1.0 O F:ASP103 4.3 35.4 1.0 OD1 F:ASP107 4.3 40.1 1.0 O F:HOH374 4.4 40.8 1.0 OG F:SER109 4.4 47.2 1.0 CB F:ASP103 4.4 35.9 1.0 OD1 F:ASP104 4.5 40.8 1.0 O16 F:ZOL354 4.5 39.5 1.0 O F:HOH367 4.5 38.2 1.0 C F:ASP103 4.6 38.9 1.0 O10 F:ZOL354 4.7 38.5 1.0 O F:HOH360 4.8 37.2 1.0 O F:HOH390 4.9 43.6 1.0 MG F:MG2 4.9 41.0 1.0 O F:HOH359 4.9 38.3 1.0

Magnesium binding site 2 out of 3 in the Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg2 b:41.0 occ:1.00 O12 F:ZOL354 2.0 38.9 1.0 O17 F:ZOL354 2.0 37.2 1.0 O F:HOH374 2.1 40.8 1.0 O F:HOH365 2.2 38.1 1.0 OD2 F:ASP243 2.2 38.6 1.0 O F:HOH363 2.3 36.2 1.0 CG F:ASP243 3.2 41.0 1.0 P14 F:ZOL354 3.3 42.0 1.0 P9 F:ZOL354 3.3 38.4 1.0 O13 F:ZOL354 3.5 38.0 1.0 C8 F:ZOL354 3.5 39.5 1.0 OD1 F:ASP243 3.5 40.4 1.0 O15 F:ZOL354 4.0 38.9 1.0 O F:HOH358 4.1 37.1 1.0 O F:HOH398 4.1 48.5 1.0 O F:HOH366 4.1 39.5 1.0 OD2 F:ASP247 4.1 47.0 1.0 O F:ASP243 4.2 42.1 1.0 NE2 F:GLN240 4.2 39.8 1.0 O11 F:ZOL354 4.2 39.2 1.0 NZ F:LYS257 4.2 45.7 1.0 OD2 F:ASP261 4.3 43.8 1.0 OD1 F:ASP261 4.4 43.0 1.0 O16 F:ZOL354 4.4 39.5 1.0 CB F:ASP243 4.4 41.1 1.0 O10 F:ZOL354 4.5 38.5 1.0 O F:HOH373 4.5 40.5 1.0 C F:ASP243 4.5 42.4 1.0 OD1 F:ASP244 4.5 38.6 1.0 CB F:ASP247 4.6 47.1 1.0 CG F:ASP247 4.7 49.6 1.0 CG F:ASP261 4.7 43.4 1.0 MG F:MG355 4.9 39.2 1.0 CE F:LYS257 4.9 49.2 1.0 N F:ASP244 4.9 40.9 1.0

Magnesium binding site 3 out of 3 in the Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Human Fpps Complex with FBS_04 and Zoledronic Acid/MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg3 b:40.3 occ:1.00 OD2 F:ASP103 2.0 39.2 1.0 O F:HOH360 2.0 37.2 1.0 O11 F:ZOL354 2.1 39.2 1.0 O F:HOH364 2.1 36.8 1.0 O F:HOH359 2.1 38.3 1.0 OD2 F:ASP107 2.2 37.7 1.0 CG F:ASP103 2.9 40.6 1.0 OD1 F:ASP103 3.1 38.9 1.0 CG F:ASP107 3.1 37.0 1.0 MG F:MG355 3.2 39.2 1.0 OD1 F:ASP107 3.3 40.1 1.0 P9 F:ZOL354 3.3 38.4 1.0 O10 F:ZOL354 3.5 38.5 1.0 OD2 F:ASP174 4.0 45.5 1.0 NE2 F:GLN171 4.1 37.0 1.0 OE1 F:GLN171 4.2 41.2 1.0 O F:HOH358 4.2 37.1 1.0 C19 F:ZOL354 4.2 38.9 1.0 CB F:ASP103 4.3 35.9 1.0 O F:HOH366 4.4 39.5 1.0 NZ F:LYS266 4.4 49.9 1.0 O12 F:ZOL354 4.4 38.9 1.0 C7 F:ZOL354 4.4 39.9 1.0 CG F:ASP174 4.4 44.4 1.0 OD1 F:ASP174 4.5 42.5 1.0 CB F:ASP107 4.5 37.5 1.0 C8 F:ZOL354 4.5 39.5 1.0 CD F:GLN171 4.6 43.6 1.0 O15 F:ZOL354 4.6 38.9 1.0 N15 F:ZOL354 4.6 38.5 1.0 O F:ASP103 4.7 35.4 1.0 NZ F:LYS200 4.8 38.0 1.0 O F:HOH361 4.9 36.1 1.0 CA F:ASP103 4.9 36.0 1.0

W.Jahnke, J.M.Rondeau, S.Cotesta, A.Marzinzik, X.Pelle, M.Geiser, A.Strauss, M.Gotte, F.Bitsch, R.Hemmig, C.Henry, S.Lehmann, J.F.Glickman, T.P.Roddy, S.J.Stout, J.R.Green. Allosteric Non-Bisphosphonate Fpps Inhibitors Identified By Fragment-Based Discovery. Nat.Chem.Biol. V. 6 660 2010.
ISSN: ISSN 1552-4450
PubMed: 20711197
DOI: 10.1038/NCHEMBIO.421