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Magnesium in PDB 5hzh: Crystal Structure of Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain

Protein crystallography data

The structure of Crystal Structure of Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain, PDB code: 5hzh was solved by M.Tarnawski, O.Dagliyan, P.H.Chu, D.Shirvanyants, N.V.Dokholyan, K.M.Hahn, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.14 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.050, 74.270, 58.400, 90.00, 94.62, 90.00
R / Rfree (%) 20.4 / 25.5

Other elements in 5hzh:

The structure of Crystal Structure of Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain (pdb code 5hzh). 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 Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain, PDB code: 5hzh:

Magnesium binding site 1 out of 1 in 5hzh

Go back to Magnesium Binding Sites List in 5hzh
Magnesium binding site 1 out of 1 in the Crystal Structure of Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain


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 Photoinhibitable RAC1 Containing C450A Mutant LOV2 Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:28.5
occ:1.00
O1G A:GTP401 2.1 49.6 1.0
OG1 A:THR17 2.2 46.7 1.0
O1B A:GTP401 2.3 39.6 1.0
O A:HOH504 2.3 23.5 1.0
O A:HOH502 2.5 18.0 1.0
O3G A:GTP401 2.6 49.8 1.0
PG A:GTP401 2.8 49.3 1.0
CB A:THR35 2.9 55.4 1.0
OG1 A:THR35 3.1 57.3 1.0
N A:THR35 3.4 58.4 1.0
CB A:THR17 3.4 48.3 1.0
PB A:GTP401 3.5 41.4 1.0
O3B A:GTP401 3.6 65.5 1.0
CA A:THR35 3.7 59.1 1.0
OD2 A:ASP206 3.7 45.4 1.0
CG2 A:THR35 4.0 55.2 1.0
O2A A:GTP401 4.0 53.3 1.0
O2G A:GTP401 4.1 49.9 1.0
N A:THR17 4.2 44.0 1.0
OD1 A:ASP206 4.2 39.9 1.0
O A:THR35 4.3 64.4 1.0
CG A:ASP206 4.3 43.0 1.0
O3A A:GTP401 4.3 31.9 1.0
CA A:THR17 4.4 46.2 1.0
CG2 A:THR17 4.4 49.9 1.0
O A:THR207 4.4 40.1 1.0
O A:ILE33 4.5 61.1 1.0
C A:THR35 4.5 61.2 1.0
C A:PRO34 4.6 59.4 1.0
O2B A:GTP401 4.6 41.7 1.0
PA A:GTP401 4.6 50.5 1.0
O1A A:GTP401 4.7 49.6 1.0
NZ A:LYS16 4.8 30.9 1.0
CA A:PRO34 4.9 59.0 1.0
CE A:LYS16 5.0 29.5 1.0

Reference:

O.Dagliyan, M.Tarnawski, P.H.Chu, D.Shirvanyants, I.Schlichting, N.V.Dokholyan, K.M.Hahn. Engineering Extrinsic Disorder to Control Protein Activity in Living Cells. Science V. 354 1441 2016.
ISSN: ESSN 1095-9203
PubMed: 27980211
DOI: 10.1126/SCIENCE.AAH3404
Page generated: Sun Sep 29 16:37:27 2024

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