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Potassium in PDB 6h42: Crystal Structure of the Human Tgt Catalytic Subunit QTRT1

Enzymatic activity of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1

All present enzymatic activity of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1, PDB code: 6h42 was solved by S.Johannsson, P.Neumann, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.25 / 2.45
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 127.700, 157.820, 47.770, 90.00, 108.46, 90.00
R / Rfree (%) 20.2 / 23.1

Other elements in 6h42:

The structure of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Bromine (Br) 2 atoms
Chlorine (Cl) 10 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1 (pdb code 6h42). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1, PDB code: 6h42:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6h42

Go back to Potassium Binding Sites List in 6h42
Potassium binding site 1 out of 2 in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:57.1
occ:0.93
O A:ARG80 2.5 74.9 1.0
O A:LEU77 2.5 57.4 1.0
O A:TYR75 2.5 60.2 1.0
O A:GLY82 2.6 69.2 1.0
CG A:GLU84 3.0 78.5 1.0
OE2 A:GLU84 3.0 87.2 1.0
CD A:GLU84 3.4 84.5 1.0
C A:TYR75 3.5 60.9 1.0
C A:ARG80 3.6 75.8 1.0
C A:LEU77 3.7 56.0 1.0
N A:GLY82 3.7 70.8 1.0
C A:GLY82 3.8 69.6 1.0
C A:PRO81 3.8 72.0 1.0
CA A:PRO81 3.8 74.9 1.0
CA A:TYR75 4.1 67.8 1.0
O A:THR74 4.2 63.8 1.0
N A:PRO81 4.2 76.6 1.0
N A:LEU77 4.3 50.2 1.0
CA A:GLY82 4.3 71.1 1.0
CB A:GLU84 4.4 74.2 1.0
O A:PRO81 4.5 71.8 1.0
C A:HIS76 4.6 52.0 1.0
N A:HIS76 4.6 56.0 1.0
CA A:GLY78 4.6 57.2 1.0
N A:GLY78 4.6 56.4 1.0
CA A:LEU77 4.6 52.4 1.0
O A:HOH647 4.7 75.1 1.0
OE1 A:GLU84 4.7 86.7 1.0
N A:ARG80 4.8 74.3 1.0
CD1 A:TYR75 4.8 96.1 1.0
CA A:ARG80 4.8 76.7 1.0
C A:GLY78 4.8 58.3 1.0
C A:PRO83 4.9 67.8 1.0
N A:PRO83 4.9 68.7 1.0
CG A:TYR75 4.9 92.8 1.0
CA A:HIS76 4.9 55.3 1.0
N A:GLU84 4.9 68.8 1.0

Potassium binding site 2 out of 2 in 6h42

Go back to Potassium Binding Sites List in 6h42
Potassium binding site 2 out of 2 in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K501

b:66.9
occ:1.00
O B:TYR75 2.4 72.3 0.9
O B:ARG80 2.4 85.7 1.0
OE1 B:GLU84 2.4 89.8 1.0
O B:LEU77 2.5 65.6 1.0
O B:GLY82 2.7 71.3 1.0
CD B:GLU84 3.3 90.0 1.0
C B:TYR75 3.5 73.3 0.9
C B:ARG80 3.6 83.7 1.0
OE2 B:GLU84 3.7 91.3 1.0
N B:GLY82 3.7 74.4 1.0
C B:LEU77 3.8 66.8 1.0
CA B:PRO81 3.8 78.6 1.0
C B:PRO81 3.8 76.8 1.0
C B:GLY82 3.8 71.9 1.0
O B:HOH651 3.9 74.2 1.0
N B:PRO81 4.1 81.1 1.0
CA B:TYR75 4.2 76.4 0.9
N B:LEU77 4.3 66.5 1.0
O B:THR74 4.4 73.4 1.0
CA B:GLY82 4.4 72.8 1.0
C B:HIS76 4.4 68.0 1.0
N B:HIS76 4.5 71.8 1.0
O B:PRO81 4.6 77.2 1.0
CG B:GLU84 4.6 88.0 1.0
CA B:LEU77 4.7 66.6 1.0
N B:GLY78 4.7 68.6 1.0
CA B:HIS76 4.7 70.1 1.0
N B:ARG80 4.7 85.8 1.0
CA B:GLY78 4.7 70.3 1.0
CA B:ARG80 4.8 86.4 1.0
O B:HIS76 4.8 67.7 1.0
C B:GLY78 4.8 71.4 1.0
CD1 B:TYR75 4.8 97.2 0.9
CG B:TYR75 4.9 93.1 0.9
CB B:GLU84 4.9 84.3 1.0
N B:PRO83 5.0 73.4 1.0

Reference:

S.Johannsson, P.Neumann, R.Ficner. Crystal Structure of the Human Trna Guanine Transglycosylase Catalytic Subunit QTRT1. Biomolecules V. 8 2018.
ISSN: ISSN 2218-273X
PubMed: 30149595
DOI: 10.3390/BIOM8030081
Page generated: Sat Aug 9 11:08:51 2025

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