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Magnesium in PDB 7pb1: Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Ggpp and Ispp

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

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

Protein crystallography data

The structure of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Ggpp and Ispp, PDB code: 7pb1 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) 45.86 / 2.59
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 183.47, 183.47, 112.29, 90, 90, 120
R / Rfree (%) 20.5 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Ggpp and Ispp (pdb code 7pb1). 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, Ggpp and Ispp, PDB code: 7pb1:

Magnesium binding site 1 out of 1 in 7pb1

Go back to Magnesium Binding Sites List in 7pb1
Magnesium binding site 1 out of 1 in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex in Complex with Magnesium, Ggpp and Ispp


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, Ggpp and Ispp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:55.6
occ:1.00
 O3B A:GRG402 1.9 67.2 1.0
O B:HOH301 2.0 56.9 1.0
OD1 A:ASP34 2.1 76.9 1.0
O7 A:ISY403 2.2 62.8 1.0
O2A A:GRG402 2.2 49.4 1.0
O A:HOH501 2.2 50.3 1.0
PB A:GRG402 3.0 86.3 1.0
CG A:ASP34 3.1 64.8 1.0
PA A:GRG402 3.2 63.6 1.0
O2B A:GRG402 3.3 72.1 1.0
OD2 A:ASP34 3.4 63.0 1.0
O3A A:GRG402 3.4 81.3 1.0
P3 A:ISY403 3.5 77.7 1.0
NH2 A:ARG38 3.6 63.3 1.0
O1 A:GRG402 3.8 49.3 1.0
O2 A:ISY403 4.0 76.8 1.0
C1 A:GRG402 4.1 67.6 1.0
N A:GLY35 4.1 57.2 1.0
NE B:ARG290 4.2 81.9 1.0
O1B A:GRG402 4.3 73.2 1.0
NH2 A:ARG85 4.3 74.8 1.0
CB A:ASP34 4.4 63.0 1.0
S9 A:ISY403 4.5 73.1 1.0
O1A A:GRG402 4.5 74.8 1.0
NH2 B:ARG290 4.6 83.4 1.0
O8 A:ISY403 4.6 78.4 1.0
O5 A:ISY403 4.7 81.7 1.0
CA A:ASP34 4.7 61.6 1.0
CZ A:ARG38 4.7 60.3 1.0
NH2 A:ARG205 4.8 72.9 1.0
CZ B:ARG290 4.9 76.7 1.0
P1 A:ISY403 4.9 68.5 1.0
CA A:GLY35 4.9 49.1 1.0
C A:ASP34 4.9 61.6 1.0
O6 A:ISY403 5.0 74.0 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 Aug 14 12:46:15 2025

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