Atomistry » Magnesium » PDB 3a0u-3abk » 3a4l
Atomistry »
  Magnesium »
    PDB 3a0u-3abk »
      3a4l »

Magnesium in PDB 3a4l: Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase

Protein crystallography data

The structure of Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase, PDB code: 3a4l was solved by Y.Araiso, R.Ishitani, D.Soll, O.Nureki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.37 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.134, 74.452, 64.698, 90.00, 113.64, 90.00
R / Rfree (%) 21 / 24.9

Other elements in 3a4l:

The structure of Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase also contains other interesting chemical elements:

Iodine (I) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase (pdb code 3a4l). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase, PDB code: 3a4l:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3a4l

Go back to Magnesium Binding Sites List in 3a4l
Magnesium binding site 1 out of 2 in the Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase


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 Archaeal O-Phosphoseryl-Trna(Sec) Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:21.4
occ:1.00
O3G A:ANP301 2.0 19.9 1.0
O1B A:ANP301 2.1 14.9 1.0
OG A:SER18 2.1 18.6 1.0
O A:HOH272 2.2 15.7 1.0
O A:HOH278 2.3 18.2 1.0
O A:HOH298 2.3 18.7 1.0
CB A:SER18 3.2 15.7 1.0
PG A:ANP301 3.2 20.2 1.0
PB A:ANP301 3.2 17.6 1.0
N3B A:ANP301 3.4 22.6 1.0
N A:SER18 3.8 18.4 1.0
O A:HOH267 3.9 31.2 1.0
O A:HOH321 4.0 26.6 1.0
CA A:SER18 4.1 17.6 1.0
O1A A:ANP301 4.1 22.4 1.0
OD1 A:ASP78 4.1 19.1 1.0
OD2 A:ASP78 4.1 21.7 1.0
O2G A:ANP301 4.1 20.5 1.0
O A:HOH345 4.2 37.7 1.0
O A:HOH361 4.3 29.8 1.0
O3A A:ANP301 4.3 19.5 1.0
O2B A:ANP301 4.3 17.0 1.0
O1G A:ANP301 4.4 25.1 1.0
CG A:ASP78 4.5 20.3 1.0
PA A:ANP301 4.5 20.5 1.0
OD1 A:ASP41 4.7 34.6 1.0
CB A:LYS17 4.7 16.0 1.0
O2A A:ANP301 4.8 18.9 1.0
C A:LYS17 4.9 17.4 1.0
CE A:LYS17 5.0 17.3 1.0

Magnesium binding site 2 out of 2 in 3a4l

Go back to Magnesium Binding Sites List in 3a4l
Magnesium binding site 2 out of 2 in the Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Archaeal O-Phosphoseryl-Trna(Sec) Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:23.4
occ:1.00
O B:HOH267 2.1 18.4 1.0
O2G B:ANP301 2.1 23.1 1.0
O1B B:ANP301 2.1 18.9 1.0
OG B:SER18 2.2 17.5 1.0
O B:HOH393 2.2 24.0 1.0
O B:HOH283 2.3 22.8 1.0
CB B:SER18 3.2 20.2 1.0
PG B:ANP301 3.3 24.0 1.0
PB B:ANP301 3.3 22.2 1.0
N3B B:ANP301 3.5 23.2 1.0
N B:SER18 3.9 18.6 1.0
OD1 B:ASP78 4.0 20.4 1.0
O B:HOH358 4.0 31.1 1.0
O1G B:ANP301 4.0 24.6 1.0
O1A B:ANP301 4.1 24.3 1.0
CA B:SER18 4.1 20.4 1.0
O B:HOH285 4.2 35.8 1.0
OD2 B:ASP78 4.2 21.9 1.0
O2B B:ANP301 4.3 20.4 1.0
O3A B:ANP301 4.4 23.8 1.0
O3G B:ANP301 4.4 26.6 1.0
CG B:ASP78 4.5 21.1 1.0
PA B:ANP301 4.6 24.3 1.0
OD2 B:ASP41 4.6 31.6 1.0
O B:HOH338 4.7 27.0 1.0
CE B:LYS17 4.8 18.2 1.0
CB B:LYS17 4.8 19.9 1.0
O2A B:ANP301 4.9 21.4 1.0
C B:LYS17 5.0 17.1 1.0

Reference:

Y.Araiso, R.L.Sherrer, R.Ishitani, J.M.L.Ho, D.Soll, O.Nureki. Structure of A Trna-Dependent Kinase Essential For Selenocysteine Decoding Proc.Natl.Acad.Sci.Usa V. 106 16215 2009.
ISSN: ISSN 0027-8424
PubMed: 19805283
DOI: 10.1073/PNAS.0908861106
Page generated: Wed Aug 14 08:27:33 2024

Last articles

F in 8FTC
F in 8FPJ
F in 8FPI
F in 8FM8
F in 8FNP
F in 8FNO
F in 8FNQ
F in 8FNN
F in 8FNL
F in 8FNM
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy