Magnesium in PDB 6qp0: Crystal Structure of Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3

Protein crystallography data

The structure of Crystal Structure of Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3, PDB code: 6qp0 was solved by R.Krutyholowa, S.Glatt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.51 / 2.41
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.020, 71.020, 88.570, 90.00, 90.00, 120.00
R / Rfree (%) 23.9 / 27.5

Other elements in 6qp0:

The structure of Crystal Structure of Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3 also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Aluminium (Al) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3 (pdb code 6qp0). 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 Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3, PDB code: 6qp0:

Magnesium binding site 1 out of 1 in 6qp0

Go back to Magnesium Binding Sites List in 6qp0
Magnesium binding site 1 out of 1 in the Crystal Structure of Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3


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 Chaetomium Thermophilum KTI12 in Complex with Adp-ALF3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:33.6
occ:1.00
OG1 A:THR15 2.0 65.0 1.0
F1 A:AF3502 2.0 39.2 1.0
O A:HOH918 2.3 49.5 1.0
O1B A:ADP501 2.7 53.6 1.0
OD1 A:ASP129 2.9 32.3 1.0
H A:THR15 3.1 56.4 1.0
OD2 A:ASP129 3.1 33.4 1.0
HB2 A:LYS14 3.2 53.8 1.0
HZ1 A:LYS14 3.3 53.4 1.0
CG A:ASP129 3.4 32.5 1.0
CB A:THR15 3.4 47.8 1.0
O A:HOH915 3.5 25.5 1.0
N A:THR15 3.5 47.0 1.0
AL A:AF3502 3.7 41.6 1.0
O3B A:ADP501 3.7 50.3 1.0
PB A:ADP501 3.8 49.7 1.0
CA A:THR15 3.8 47.4 1.0
HB A:THR15 3.8 57.3 1.0
HA A:THR15 3.8 56.8 1.0
O A:HOH933 3.9 48.8 1.0
HB3 A:LYS14 4.0 53.8 1.0
CB A:LYS14 4.1 44.9 1.0
NZ A:LYS14 4.1 44.5 1.0
HZ3 A:LYS14 4.1 53.4 1.0
CG2 A:THR15 4.3 48.0 1.0
HG23 A:THR15 4.3 57.6 1.0
O2B A:ADP501 4.4 44.3 1.0
C A:LYS14 4.4 46.8 1.0
HG21 A:THR15 4.4 57.6 1.0
HD2 A:LYS14 4.4 51.6 1.0
F3 A:AF3502 4.5 41.2 1.0
HB2 A:SER76 4.5 58.4 1.0
HZ2 A:LYS14 4.5 53.4 1.0
O A:ASP129 4.6 35.3 1.0
HH A:TYR74 4.7 47.3 1.0
CA A:LYS14 4.8 46.5 1.0
CB A:ASP129 4.8 31.8 1.0
HA A:SER130 4.8 45.0 1.0
F2 A:AF3502 4.8 41.2 1.0
HH21 A:ARG84 4.9 61.2 1.0
H A:LYS14 5.0 57.4 1.0
C A:ASP129 5.0 33.6 1.0

Reference:

R.Krutyholowa, A.Hammermeister, R.Zabel, W.Abdel-Fattah, A.Reinhardt-Tews, M.Helm, M.J.R.Stark, K.D.Breunig, R.Schaffrath, S.Glatt. KTI12, A Pstk-Like Trna Dependent Atpase Essential For Trna Modification By Elongator. Nucleic Acids Res. V. 47 4814 2019.
ISSN: ESSN 1362-4962
PubMed: 30916349
DOI: 10.1093/NAR/GKZ190
Page generated: Mon Dec 14 23:52:52 2020

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