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Magnesium in PDB 1i0i: Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant

Enzymatic activity of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant

All present enzymatic activity of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant:
2.4.2.8;

Protein crystallography data

The structure of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant, PDB code: 1i0i was solved by B.Canyuk, P.J.Focia, A.E.Eakin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.380, 101.270, 51.670, 90.00, 94.25, 90.00
R / Rfree (%) 16.8 / 25.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant (pdb code 1i0i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant, PDB code: 1i0i:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1i0i

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Magnesium binding site 1 out of 4 in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg900

b:27.6
occ:1.00
O A:HOH1302 2.1 16.1 1.0
O A:HOH1301 2.1 24.5 1.0
O3B A:PRP801 2.1 22.6 1.0
O2 A:PRP801 2.4 33.0 1.0
O3 A:PRP801 2.6 39.3 1.0
O1 A:PRP801 2.8 26.1 1.0
C2 A:PRP801 3.3 34.5 1.0
PB A:PRP801 3.3 21.6 1.0
C3 A:PRP801 3.3 36.4 1.0
O3A A:PRP801 3.4 25.4 1.0
OE2 A:GLU111 3.5 26.3 1.0
OD1 A:ASP112 3.7 29.5 1.0
C1 A:PRP801 3.7 32.4 1.0
OE1 A:GLU111 3.7 26.5 1.0
PA A:PRP801 3.8 21.9 1.0
O A:LEU51 3.9 13.3 1.0
N A:GLY53 4.0 10.4 1.0
CD A:GLU111 4.0 24.7 1.0
OD2 A:ASP112 4.1 33.5 1.0
O2B A:PRP801 4.2 18.2 1.0
N A:LYS52 4.2 14.2 1.0
O A:VAL50 4.3 16.5 1.0
CG A:ASP112 4.3 30.4 1.0
O1B A:PRP801 4.3 20.6 1.0
C A:LEU51 4.3 14.7 1.0
CA A:GLY53 4.4 12.4 1.0
O4 A:PRP801 4.4 35.4 1.0
C4 A:PRP801 4.5 38.3 1.0
CG1 A:VAL50 4.6 8.6 1.0
O1A A:PRP801 4.7 20.4 1.0
O2A A:PRP801 4.8 20.5 1.0
O A:HOH1305 4.9 27.3 1.0

Magnesium binding site 2 out of 4 in 1i0i

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Magnesium binding site 2 out of 4 in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:26.0
occ:1.00
O A:HOH1303 2.0 23.8 1.0
OD1 A:ASP171 2.0 27.0 1.0
O A:HOH1305 2.1 27.3 1.0
O A:HOH1304 2.1 28.5 1.0
O2A A:PRP801 2.2 20.5 1.0
O1B A:PRP801 2.3 20.6 1.0
CG A:ASP171 3.0 23.9 1.0
OD2 A:ASP171 3.2 24.8 1.0
PA A:PRP801 3.4 21.9 1.0
PB A:PRP801 3.5 21.6 1.0
O3A A:PRP801 3.7 25.4 1.0
NH2 A:ARG177 3.9 6.4 1.0
O1 A:PRP801 4.0 26.1 1.0
O A:HOH1070 4.0 36.8 1.0
NH1 A:ARG177 4.1 8.6 1.0
O A:ASP171 4.2 17.8 1.0
O3B A:PRP801 4.3 22.6 1.0
CB A:ASP171 4.3 16.2 1.0
C1 A:PRP801 4.4 32.4 1.0
CZ A:ARG177 4.5 9.4 1.0
O2 A:PRP801 4.5 33.0 1.0
O A:HOH1073 4.5 25.6 1.0
N3 A:7HP800 4.5 26.5 1.0
O1A A:PRP801 4.5 20.4 1.0
N A:ASP171 4.6 11.7 1.0
O A:HOH1071 4.6 23.2 1.0
O2B A:PRP801 4.6 18.2 1.0
C A:ASP171 4.7 19.8 1.0
CA A:ASP171 4.8 17.5 1.0
C2 A:PRP801 5.0 34.5 1.0

Magnesium binding site 3 out of 4 in 1i0i

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Magnesium binding site 3 out of 4 in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg912

b:15.3
occ:1.00
O2A B:PRP811 2.0 10.9 1.0
O B:HOH1308 2.1 11.1 1.0
O B:HOH1307 2.1 13.8 1.0
O B:HOH1306 2.1 9.7 1.0
OD1 B:ASP171 2.2 15.0 1.0
O1B B:PRP811 2.4 16.7 1.0
CG B:ASP171 3.0 10.9 1.0
OD2 B:ASP171 3.1 8.9 1.0
PA B:PRP811 3.2 13.1 1.0
PB B:PRP811 3.4 11.9 1.0
O3A B:PRP811 3.5 16.6 1.0
O B:HOH1031 3.6 23.0 1.0
O1 B:PRP811 3.8 13.1 1.0
O B:HOH1025 3.8 22.3 1.0
NH2 B:ARG177 4.0 9.0 1.0
O B:HOH1022 4.1 21.0 1.0
O B:ASP171 4.2 17.2 1.0
C1 B:PRP811 4.2 13.1 1.0
O2B B:PRP811 4.4 16.1 1.0
CB B:TYR82 4.4 21.3 1.0
O1A B:PRP811 4.4 13.8 1.0
O B:GLY83 4.4 15.6 1.0
N3 B:7HP810 4.5 14.4 1.0
O3B B:PRP811 4.5 11.3 1.0
CB B:ASP171 4.5 9.7 1.0
NH1 B:ARG177 4.5 12.2 1.0
CZ B:ARG177 4.7 11.5 1.0
O B:HOH1024 4.7 10.2 1.0
C B:ASP171 4.7 14.3 1.0
N B:ASP171 4.8 8.1 1.0
O2 B:PRP811 4.9 17.6 1.0
CA B:ASP171 5.0 11.1 1.0

Magnesium binding site 4 out of 4 in 1i0i

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Magnesium binding site 4 out of 4 in the Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Analysis of An Invariant Aspartic Acid in Hprts-Glutamine Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg910

b:14.8
occ:1.00
O B:HOH1310 2.0 13.4 1.0
O B:HOH1309 2.0 10.9 1.0
O3 B:PRP811 2.2 16.4 1.0
O2 B:PRP811 2.3 17.6 1.0
O3B B:PRP811 2.3 11.3 1.0
O1 B:PRP811 2.7 13.1 1.0
C3 B:PRP811 3.1 12.0 1.0
C2 B:PRP811 3.1 14.4 1.0
PB B:PRP811 3.4 11.9 1.0
O3A B:PRP811 3.5 16.6 1.0
C1 B:PRP811 3.5 13.1 1.0
OE1 B:GLU111 3.8 15.7 1.0
OE2 B:GLU111 3.8 13.6 1.0
PA B:PRP811 3.8 13.1 1.0
OD1 B:ASP112 3.9 14.7 1.0
O B:HOH1027 4.1 10.6 1.0
C4 B:PRP811 4.1 13.7 1.0
O B:LEU51 4.2 11.1 1.0
CD B:GLU111 4.2 13.3 1.0
O B:VAL50 4.3 14.0 1.0
O1B B:PRP811 4.3 16.7 1.0
O4 B:PRP811 4.3 12.2 1.0
CG1 B:VAL50 4.3 9.4 1.0
N B:GLY53 4.4 10.0 1.0
O2B B:PRP811 4.4 16.1 1.0
O B:HOH1031 4.5 23.0 1.0
O1A B:PRP811 4.6 13.8 1.0
CA B:GLY53 4.6 9.3 1.0
C B:LEU51 4.6 11.7 1.0
O B:VAL79 4.6 15.1 1.0
N B:LYS52 4.7 13.6 1.0
CG B:ASP112 4.8 12.3 1.0
O2A B:PRP811 4.9 10.9 1.0
OD2 B:ASP112 4.9 19.3 1.0
CB B:VAL50 5.0 9.9 1.0

Reference:

B.Canyuk, P.J.Focia, A.E.Eakin. The Role For An Invariant Aspartic Acid in Hypoxanthine Phosphoribosyltransferases Is Examined Using Saturation Mutagenesis, Functional Analysis, and X-Ray Crystallography. Biochemistry V. 40 2754 2001.
ISSN: ISSN 0006-2960
PubMed: 11258886
DOI: 10.1021/BI001195Q
Page generated: Tue Aug 13 04:33:07 2024

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