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Magnesium in PDB 5iit: Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1

Protein crystallography data

The structure of Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1, PDB code: 5iit was solved by R.Wild, M.Hothorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.86 / 2.13
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 105.640, 67.922, 129.677, 90.00, 93.32, 90.00
R / Rfree (%) 21.1 / 24.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1 (pdb code 5iit). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1, PDB code: 5iit:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5iit

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Magnesium binding site 1 out of 2 in the Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg404

b:61.0
occ:1.00
O B:GLY263 2.2 63.8 1.0
O B:LEU266 2.3 61.2 1.0
O B:HOH543 2.4 54.2 1.0
O B:ALA268 2.4 49.8 1.0
O B:HOH551 2.6 72.2 1.0
C B:GLY263 3.2 60.7 1.0
C B:ALA268 3.5 49.9 1.0
C B:LEU266 3.5 58.5 1.0
CA B:GLY263 3.8 54.7 1.0
CA B:LYS269 4.0 50.4 1.0
N B:LEU266 4.1 55.3 1.0
N B:LYS269 4.1 50.7 1.0
C B:PRO267 4.1 54.5 1.0
O B:PRO267 4.2 56.0 1.0
CA B:LEU266 4.2 53.9 1.0
O B:LYS269 4.3 54.6 1.0
N B:HIS264 4.3 61.9 1.0
N B:ALA268 4.3 50.2 1.0
C B:LYS269 4.4 48.2 1.0
CB B:LEU266 4.4 49.8 1.0
N B:PRO267 4.5 57.2 1.0
N B:GLY263 4.5 56.5 1.0
CA B:ALA268 4.5 50.1 1.0
CA B:HIS264 4.6 64.8 1.0
CA B:PRO267 4.6 57.2 1.0
N B:GLY265 4.9 66.2 1.0
C B:HIS264 5.0 66.9 1.0

Magnesium binding site 2 out of 2 in 5iit

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Magnesium binding site 2 out of 2 in the Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Spx Domain of the Yeast Inorganic Polyphophate Polymerase VTC4 Crystallized By Carrier-Driven Crystallization in Fusion with the Macro Domain of Human Histone MACROH2A1.1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg405

b:73.6
occ:1.00
O C:HOH544 2.6 60.4 1.0
O C:ALA268 2.7 69.9 1.0
O C:LEU266 2.7 63.4 1.0
O C:GLY263 2.8 79.4 1.0
C C:ALA268 3.5 63.8 1.0
CA C:LYS269 3.6 64.5 1.0
C C:GLY263 3.8 76.2 1.0
C C:LEU266 3.9 64.5 1.0
N C:LYS269 3.9 60.5 1.0
O C:PRO267 4.1 69.9 1.0
O C:LYS269 4.2 64.2 1.0
C C:LYS269 4.3 61.3 1.0
CA C:GLY263 4.3 72.0 1.0
C C:PRO267 4.3 65.3 1.0
N C:ALA268 4.6 57.6 1.0
N C:LEU266 4.6 68.9 1.0
CA C:ALA268 4.7 58.8 1.0
CB C:LYS269 4.7 66.4 1.0
CA C:LEU266 4.7 65.9 1.0
CG C:LYS269 4.8 72.4 1.0
N C:GLY263 4.8 69.2 1.0
N C:HIS264 4.8 78.2 1.0
N C:PRO267 4.8 65.5 1.0
CA C:PRO267 4.9 68.5 1.0

Reference:

R.Wild, R.Gerasimaite, J.Y.Jung, V.Truffault, I.Pavlovic, A.Schmidt, A.Saiardi, H.J.Jessen, Y.Poirier, M.Hothorn, A.Mayer. Control of Eukaryotic Phosphate Homeostasis By Inositol Polyphosphate Sensor Domains. Science V. 352 986 2016.
ISSN: ESSN 1095-9203
PubMed: 27080106
DOI: 10.1126/SCIENCE.AAD9858
Page generated: Sun Sep 29 16:42:29 2024

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