Magnesium in PDB 7pax: Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp

Enzymatic activity of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp

All present enzymatic activity of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp:
2.5.1.87;

Protein crystallography data

The structure of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp, PDB code: 7pax was solved by M.Giladi, M.Lisnyansky Bar-El, Y.Haitin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.13 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 183.987, 183.987, 112.537, 90, 90, 120
R / Rfree (%) 20.5 / 23.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp (pdb code 7pax). 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 Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp, PDB code: 7pax:

Magnesium binding site 1 out of 1 in 7pax

Go back to Magnesium Binding Sites List in 7pax
Magnesium binding site 1 out of 1 in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Fspp and Ipp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:45.7
occ:1.00
 O A:HOH515 2.0 50.8 1.0
OD1 A:ASP34 2.1 64.3 1.0
O A:HOH508 2.2 42.3 1.0
O3B A:FPS402 2.2 50.0 1.0
O2A A:FPS402 2.2 50.0 1.0
O1A A:IPE401 2.2 43.5 1.0
CG A:ASP34 3.1 59.8 1.0
PB A:FPS402 3.3 60.6 1.0
PA A:FPS402 3.3 60.3 1.0
OD2 A:ASP34 3.5 53.1 1.0
PA A:IPE401 3.6 49.8 1.0
O1B A:FPS402 3.7 66.8 1.0
O3A A:FPS402 3.7 58.3 1.0
NH2 A:ARG38 3.9 43.9 1.0
O1 A:IPE401 4.1 47.9 1.0
O A:HOH512 4.1 50.9 1.0
S1 A:FPS402 4.1 53.3 1.0
NH2 A:ARG85 4.1 54.9 1.0
O1B A:IPE401 4.2 50.6 1.0
N A:GLY35 4.3 52.4 1.0
CB A:ASP34 4.4 48.8 1.0
O3A A:IPE401 4.5 44.3 1.0
NH2 B:ARG290 4.5 53.2 1.0
O2A A:IPE401 4.5 50.3 1.0
NE B:ARG290 4.6 58.8 1.0
O1A A:FPS402 4.6 54.6 1.0
O2B A:FPS402 4.6 51.7 1.0
C1 A:FPS402 4.6 48.3 1.0
NH2 A:ARG205 4.6 50.2 1.0
CA A:ASP34 4.7 48.8 1.0
PB A:IPE401 4.8 50.0 1.0
O2B A:IPE401 4.9 54.7 1.0
CZ A:ARG38 5.0 49.3 1.0

Reference:

M.Giladi, M.Lisnyansky Bar-El, P.Vankova, A.Ferofontov, E.Melvin, S.Alkaderi, D.Kavan, B.Redko, E.Haimov, R.Wiener, P.Man, Y.Haitin. Structural Basis For Long-Chain Isoprenoid Synthesis By Cis -Prenyltransferases. Sci Adv V. 8 N1171 2022.
ISSN: ESSN 2375-2548
PubMed: 35584224
DOI: 10.1126/SCIADV.ABN1171
Page generated: Thu Oct 3 04:03:10 2024

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