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Magnesium in PDB 1z5v: Crystal Structure of Human Gamma-Tubulin Bound to Gtpgammas

Protein crystallography data

The structure of Crystal Structure of Human Gamma-Tubulin Bound to Gtpgammas, PDB code: 1z5v was solved by H.A.Aldaz, L.M.Rice, T.Stearns, D.A.Agard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.04 / 2.71
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.427, 76.325, 65.197, 90.00, 101.93, 90.00
R / Rfree (%) 23.7 / 29.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Gamma-Tubulin Bound to Gtpgammas (pdb code 1z5v). 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 Crystal Structure of Human Gamma-Tubulin Bound to Gtpgammas, PDB code: 1z5v:

Magnesium binding site 1 out of 1 in 1z5v

Go back to Magnesium Binding Sites List in 1z5v
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Gamma-Tubulin Bound to Gtpgammas


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 Human Gamma-Tubulin Bound to Gtpgammas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg475

b:55.2
occ:1.00
O2G A:GSP2466 1.9 59.9 1.0
O2B A:GSP2466 2.7 46.4 1.0
PG A:GSP2466 3.2 59.4 1.0
O3B A:GSP2466 3.3 54.0 1.0
PB A:GSP2466 3.3 47.9 1.0
OD1 A:ASP68 3.7 38.6 1.0
OG1 A:THR145 3.9 40.1 1.0
O1B A:GSP2466 4.0 46.6 1.0
N A:GLN12 4.0 38.5 1.0
O A:HOH2479 4.0 55.8 1.0
OE1 A:GLU70 4.3 57.9 1.0
S1G A:GSP2466 4.4 65.3 1.0
O3G A:GSP2466 4.4 60.2 1.0
CA A:GLY11 4.4 37.1 1.0
OD2 A:ASP68 4.5 43.4 1.0
CB A:GLN12 4.6 44.3 1.0
CG A:ASP68 4.6 41.4 1.0
CB A:THR145 4.6 39.7 1.0
O3A A:GSP2466 4.7 49.8 1.0
CB A:GLU70 4.7 52.0 1.0
C A:GLY11 4.7 38.1 1.0
CA A:GLN12 4.9 41.4 1.0

Reference:

H.Aldaz, L.M.Rice, T.Stearns, D.A.Agard. Insights Into Microtubule Nucleation From the Crystal Structure of Human Gamma-Tubulin. Nature V. 435 523 2005.
ISSN: ISSN 0028-0836
PubMed: 15917813
DOI: 10.1038/NATURE03586
Page generated: Tue Aug 13 20:03:55 2024

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