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Magnesium in PDB 1esq: Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.

Enzymatic activity of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.

All present enzymatic activity of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.:
2.7.1.50;

Protein crystallography data

The structure of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate., PDB code: 1esq was solved by N.Campobasso, I.I.Mathews, T.P.Begley, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.080, 100.840, 72.510, 90.00, 95.10, 90.00
R / Rfree (%) 20.9 / 28.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. (pdb code 1esq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate., PDB code: 1esq:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in 1esq

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Magnesium binding site 1 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


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 Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg340

b:32.1
occ:1.00
 O1B A:ATP300 1.9 40.1 1.0
O2 A:TZP320 2.3 31.2 1.0
O A:HOH575 2.5 18.9 1.0
PB A:ATP300 3.0 39.2 1.0
O2B A:ATP300 3.3 38.9 1.0
P1 A:TZP320 3.6 33.2 1.0
O3 A:TZP320 3.7 31.4 1.0
NH2 A:ARG121 3.7 24.7 1.0
O3B A:ATP300 3.8 37.7 1.0
CG2 A:VAL96 4.0 23.5 1.0
OE1 A:GLU126 4.1 32.7 1.0
OD1 A:ASP94 4.1 26.2 1.0
O1 A:TZP320 4.3 33.7 1.0
O3A A:ATP300 4.3 39.2 1.0
O2G A:ATP300 4.4 36.0 1.0
OE2 A:GLU126 4.4 29.3 1.0
CG1 A:VAL96 4.4 22.9 1.0
O7 A:TZP320 4.5 31.5 1.0
OD2 A:ASP94 4.6 25.7 1.0
CB A:VAL96 4.6 26.0 1.0
CA A:GLY197 4.6 23.2 1.0
CD A:GLU126 4.7 32.4 1.0
CZ A:ARG121 4.7 27.3 1.0
PG A:ATP300 4.7 35.5 1.0
CA A:VAL96 4.7 25.9 1.0
CG A:ASP94 4.8 26.5 1.0
NH1 A:ARG121 4.8 26.6 1.0
N A:SER198 5.0 21.6 1.0
C7 A:TZP320 5.0 26.2 1.0

Magnesium binding site 2 out of 6 in 1esq

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Magnesium binding site 2 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


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 Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg365

b:46.5
occ:1.00
 O3G A:ATP300 2.0 36.8 1.0
O2B A:ATP300 2.0 38.9 1.0
O1 A:TZP320 3.2 33.7 1.0
PG A:ATP300 3.2 35.5 1.0
PB A:ATP300 3.3 39.2 1.0
O3B A:ATP300 3.5 37.7 1.0
O2G A:ATP300 3.6 36.0 1.0
O3A A:ATP300 3.9 39.2 1.0
O1A A:ATP300 4.2 39.1 1.0
O2 A:TZP320 4.2 31.2 1.0
P1 A:TZP320 4.3 33.2 1.0
O1B A:ATP300 4.5 40.1 1.0
O1G A:ATP300 4.6 36.6 1.0
PA A:ATP300 4.9 41.0 1.0
O A:VAL193 4.9 24.8 1.0
CA A:THR191 4.9 33.7 1.0
O A:THR191 4.9 35.6 1.0
O A:LEU190 4.9 35.1 1.0

Magnesium binding site 3 out of 6 in 1esq

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Magnesium binding site 3 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg345

b:22.2
occ:1.00
 O1B B:ATP305 2.3 40.8 1.0
O2 B:TZP325 2.4 32.8 1.0
O B:HOH505 2.6 23.7 1.0
O B:HOH497 2.8 18.0 1.0
PB B:ATP305 3.2 40.2 1.0
OE2 B:GLU126 3.4 30.3 1.0
O2B B:ATP305 3.5 39.9 1.0
O3B B:ATP305 3.5 41.3 1.0
O2G B:ATP305 3.7 42.5 1.0
P1 B:TZP325 3.8 35.1 1.0
OE1 B:GLU126 4.0 26.9 1.0
CG1 B:VAL96 4.1 20.0 1.0
CD B:GLU126 4.1 28.5 1.0
PG B:ATP305 4.2 42.5 1.0
NH2 B:ARG121 4.2 26.4 1.0
O3 B:TZP325 4.3 32.7 1.0
O1 B:TZP325 4.5 34.4 1.0
OD1 B:ASP94 4.6 17.6 1.0
CA B:VAL96 4.6 20.9 1.0
O7 B:TZP325 4.6 32.6 1.0
CG2 B:VAL96 4.6 18.2 1.0
CB B:VAL96 4.7 20.7 1.0
O3A B:ATP305 4.7 40.8 1.0
C7 B:TZP325 4.8 27.0 1.0
NH1 B:ARG121 4.9 26.2 1.0
ND2 B:ASN123 5.0 24.4 1.0

Magnesium binding site 4 out of 6 in 1esq

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Magnesium binding site 4 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg360

b:48.6
occ:1.00
 O2B B:ATP305 2.1 39.9 1.0
O3G B:ATP305 2.1 41.3 1.0
PB B:ATP305 3.1 40.2 1.0
O1A B:ATP305 3.2 39.6 1.0
O3A B:ATP305 3.3 40.8 1.0
PG B:ATP305 3.3 42.5 1.0
O3B B:ATP305 3.3 41.3 1.0
O1 B:TZP325 3.7 34.4 1.0
O2G B:ATP305 3.9 42.5 1.0
PA B:ATP305 4.0 41.3 1.0
O B:LEU190 4.2 29.0 1.0
O1B B:ATP305 4.4 40.8 1.0
CA B:THR191 4.5 27.7 1.0
CB B:ALA196 4.6 18.3 1.0
O1G B:ATP305 4.6 42.9 1.0
N B:GLY197 4.7 18.8 1.0
O B:THR191 4.8 25.4 1.0
O2 B:TZP325 4.8 32.8 1.0
O5' B:ATP305 4.9 37.7 1.0
P1 B:TZP325 4.9 35.1 1.0
O B:HOH574 4.9 19.1 1.0
C B:LEU190 4.9 27.7 1.0
C5' B:ATP305 5.0 37.8 1.0
O B:VAL193 5.0 21.8 1.0

Magnesium binding site 5 out of 6 in 1esq

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Magnesium binding site 5 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg350

b:41.5
occ:1.00
 O1B C:ATP310 1.9 33.2 1.0
O3 C:TZP330 2.1 29.2 1.0
O C:HOH480 2.4 20.7 1.0
NH2 C:ARG121 3.2 35.0 1.0
PB C:ATP310 3.2 33.8 1.0
P1 C:TZP330 3.3 30.0 1.0
O1 C:TZP330 3.3 31.6 1.0
O2B C:ATP310 3.5 35.1 1.0
OD1 C:ASP94 3.8 24.5 1.0
CG2 C:VAL96 4.1 18.9 1.0
O3B C:ATP310 4.1 34.5 1.0
OD2 C:ASP94 4.1 24.6 1.0
O2 C:TZP330 4.1 32.1 1.0
O7 C:TZP330 4.3 29.0 1.0
CA C:GLY197 4.4 22.0 1.0
O3A C:ATP310 4.4 32.9 1.0
CG C:ASP94 4.4 26.0 1.0
CZ C:ARG121 4.4 35.9 1.0
OE1 C:GLU126 4.5 32.4 1.0
CG1 C:VAL96 4.5 20.4 1.0
OE2 C:GLU126 4.5 31.6 1.0
N C:SER198 4.5 19.9 1.0
C C:GLY197 4.5 20.8 1.0
C7 C:TZP330 4.7 27.1 1.0
CB C:VAL96 4.7 24.0 1.0
OG C:SER198 4.7 22.0 1.0
O2G C:ATP310 4.8 31.1 1.0
NH1 C:ARG121 4.9 35.7 1.0
CD C:GLU126 5.0 31.4 1.0
CA C:VAL96 5.0 24.1 1.0

Magnesium binding site 6 out of 6 in 1esq

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Magnesium binding site 6 out of 6 in the Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Thiazole Kinase Mutant (C198S) with Atp and Thiazole Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg355

b:40.3
occ:1.00
 O3G C:ATP310 2.2 33.9 1.0
O2B C:ATP310 2.3 35.1 1.0
O1A C:ATP310 3.1 31.1 1.0
PB C:ATP310 3.2 33.8 1.0
O3A C:ATP310 3.3 32.9 1.0
PG C:ATP310 3.4 33.0 1.0
O3B C:ATP310 3.4 34.5 1.0
O C:LEU190 3.8 26.8 1.0
O2 C:TZP330 3.8 32.1 1.0
PA C:ATP310 4.0 31.1 1.0
O2G C:ATP310 4.2 31.1 1.0
CA C:THR191 4.3 24.7 1.0
CB C:ALA196 4.5 19.4 1.0
O1G C:ATP310 4.6 32.7 1.0
O1B C:ATP310 4.6 33.2 1.0
O C:VAL193 4.7 21.3 1.0
C C:LEU190 4.7 26.2 1.0
O C:THR191 4.7 25.0 1.0
N C:GLY197 4.7 21.8 1.0
O3 C:TZP330 4.8 29.2 1.0
O5' C:ATP310 4.8 30.0 1.0
C C:THR191 4.8 24.2 1.0
C5' C:ATP310 4.9 29.4 1.0
N C:THR191 4.9 25.4 1.0

Reference:

N.Campobasso, I.I.Mathews, T.P.Begley, S.E.Ealick. Crystal Structure of 4-Methyl-5-Beta-Hydroxyethylthiazole Kinase From Bacillus Subtilis at 1.5 A Resolution. Biochemistry V. 39 7868 2000.
ISSN: ISSN 0006-2960
PubMed: 10891066
DOI: 10.1021/BI0000061
Page generated: Sat Aug 9 20:48:04 2025

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