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Magnesium in PDB 1rtz: Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution

Enzymatic activity of Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution

All present enzymatic activity of Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution:
2.7.6.3;

Protein crystallography data

The structure of Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution, PDB code: 1rtz was solved by J.Blaszczyk, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.60 / 1.33
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.266, 41.685, 77.896, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 16.7

Other elements in 1rtz:

The structure of Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution (pdb code 1rtz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution, PDB code: 1rtz:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1rtz

Go back to Magnesium Binding Sites List in 1rtz
Magnesium binding site 1 out of 3 in the Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution


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 E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg161

b:23.1
occ:0.50
OD1 A:ASP95 1.9 23.1 0.5
O1 A:GOL172 2.0 24.0 0.5
O A:HOH396 2.0 21.4 0.5
O A:HOH397 2.1 23.1 0.5
O A:HOH219 2.1 16.8 1.0
OD1 A:ASP97 2.3 16.9 0.5
OD2 A:ASP97 2.3 25.8 0.5
C1 A:GOL172 2.7 27.4 0.5
CG A:ASP95 2.8 20.5 0.5
OD2 A:ASP97 2.9 28.0 0.5
CG A:ASP97 2.9 20.0 0.5
CG A:ASP97 2.9 22.2 0.5
OD1 A:ASP97 2.9 26.9 0.5
OD2 A:ASP95 3.1 26.7 0.5
O A:HOH388 3.4 24.6 0.5
O A:HOH371 3.7 33.6 1.0
O2 A:GOL172 3.8 42.2 0.5
C2 A:GOL172 3.9 29.2 0.5
O A:HOH326 3.9 33.5 1.0
O A:LEU96 4.1 11.1 1.0
CB A:ASP95 4.2 15.7 1.0
OE2 A:GLU77 4.2 10.9 1.0
CG A:ASP95 4.3 16.5 0.5
CB A:ASP97 4.4 14.2 1.0
OD1 A:ASP95 4.4 18.9 0.5
O A:HOH391 4.5 21.0 0.5
C A:LEU96 4.6 9.5 1.0
N A:LEU96 4.7 7.5 1.0
CA A:ASP95 4.7 8.6 1.0
C3 A:GOL172 4.8 33.9 0.5
O A:HOH255 4.8 19.3 1.0
CA A:ASP97 4.9 9.8 1.0
C A:ASP95 4.9 7.9 1.0
OD2 A:ASP95 4.9 21.0 0.5
N A:ASP97 4.9 8.8 1.0
O A:HOH226 5.0 17.8 1.0

Magnesium binding site 2 out of 3 in 1rtz

Go back to Magnesium Binding Sites List in 1rtz
Magnesium binding site 2 out of 3 in the Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution


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 E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg162

b:18.3
occ:0.50
O A:HOH402 2.1 33.6 0.5
O A:HOH390 2.1 18.1 0.5
O A:HOH401 2.1 35.2 0.5
O A:HOH306 2.2 26.6 1.0
OE2 A:GLU141 2.3 28.7 0.5
O A:HOH392 2.3 23.6 0.5
CD A:GLU141 3.2 26.4 0.5
OE1 A:GLU141 3.4 24.0 0.5
OE1 A:GLU141 3.6 27.4 0.5
CD A:GLU141 3.6 26.0 0.5
OE2 A:GLU141 3.6 25.6 0.5
O A:HOH380 4.1 49.1 1.0
CG A:GLU141 4.4 26.7 0.5
OD2 A:ASP139 4.6 13.9 1.0
O A:HOH381 4.6 38.3 1.0
CG A:GLU141 4.6 26.7 0.5
O A:HOH389 4.6 24.4 0.5

Magnesium binding site 3 out of 3 in 1rtz

Go back to Magnesium Binding Sites List in 1rtz
Magnesium binding site 3 out of 3 in the Crystal Structure of E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution


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 E.Coli Apo-Hppk(V83G/DEL84-89) at 1.33 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg163

b:23.2
occ:1.00
O A:HOH247 2.1 23.4 1.0
O A:HOH393 2.2 20.7 0.5
O A:GLY26 2.4 12.5 1.0
O A:HOH231 2.4 24.1 1.0
O A:SER31 2.5 10.6 1.0
O A:HOH319 2.5 39.7 1.0
O A:HOH291 3.2 46.1 1.0
C A:GLY26 3.5 9.3 1.0
O A:HOH284 3.7 62.4 1.0
C A:SER31 3.7 8.6 1.0
CB A:HIS32 4.0 10.2 1.0
CA A:HIS32 4.0 8.4 1.0
O A:HOH383 4.0 48.3 1.0
O A:ILE28 4.2 10.0 1.0
CA A:ASP27 4.3 10.4 1.0
O A:HOH310 4.3 32.6 1.0
N A:ASP27 4.3 8.7 1.0
N A:HIS32 4.3 8.3 1.0
O A:HOH208 4.5 14.2 1.0
CA A:GLY26 4.6 8.8 1.0
C A:ASP27 4.7 9.1 1.0
CA A:SER31 4.8 10.1 1.0
OD1 A:ASP27 4.8 33.2 1.0
N A:SER31 4.9 10.5 1.0

Reference:

J.Blaszczyk, Y.Li, Y.Wu, G.Shi, X.Ji, H.Yan. Essential Roles of A Dynamic Loop in the Catalysis of 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase. Biochemistry V. 43 1469 2004.
ISSN: ISSN 0006-2960
PubMed: 14769023
DOI: 10.1021/BI036053L
Page generated: Tue Aug 13 13:08:02 2024

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