Magnesium in PDB 1ol5: Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43

All present enzymatic activity of Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43:
2.7.1.37;

The structure of Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43, PDB code: 1ol5 was solved by R.Bayliss, E.Conti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40 / 2.5
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.630, 81.720, 83.050, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 25.2

The binding sites of Magnesium atom in the Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43 (pdb code 1ol5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43, PDB code: 1ol5:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1389 b:19.0 occ:1.00 O A:HOH2073 2.0 13.6 1.0 OD2 A:ASP274 2.1 17.9 1.0 OD1 A:ASN261 2.2 11.7 1.0 O3A A:ADP1388 2.4 28.1 1.0 O2A A:ADP1388 2.5 26.8 1.0 PA A:ADP1388 3.0 18.4 1.0 O3B A:ADP1388 3.1 31.9 1.0 CG A:ASP274 3.1 19.3 1.0 CG A:ASN261 3.3 12.4 1.0 PB A:ADP1388 3.4 20.9 1.0 CB A:ASP274 3.7 17.0 1.0 ND2 A:ASN261 3.8 11.2 1.0 O2B A:ADP1388 3.9 26.1 1.0 O5' A:ADP1388 4.0 22.2 1.0 C5' A:ADP1388 4.1 20.7 1.0 OD1 A:ASP274 4.2 22.4 1.0 O A:HOH2123 4.3 17.5 1.0 O1A A:ADP1388 4.3 27.0 1.0 O A:GLU260 4.3 18.7 1.0 O A:HOH2122 4.3 24.0 1.0 O3' A:ADP1388 4.5 18.8 1.0 CB A:ASN261 4.5 12.7 1.0 O1B A:ADP1388 4.6 32.3 1.0 CA A:ASN261 4.7 14.1 1.0 C A:GLU260 4.8 18.8 1.0 C3' A:ADP1388 4.8 17.8 1.0 OD2 A:ASP256 4.8 20.0 1.0

Magnesium binding site 2 out of 3 in the Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1390 b:21.2 occ:1.00 O A:HOH2026 1.8 25.6 1.0 O A:HOH2124 2.0 12.4 1.0 O2B A:ADP1388 2.1 26.1 1.0 O A:HOH2123 2.3 17.5 1.0 O A:HOH2125 2.4 17.1 1.0 O A:HOH2028 2.7 30.5 1.0 PB A:ADP1388 3.5 20.9 1.0 OD1 A:ASP274 3.7 22.4 1.0 NZ A:LYS162 4.2 21.8 1.0 O3A A:ADP1388 4.2 28.1 1.0 O1B A:ADP1388 4.3 32.3 1.0 OE1 A:GLU181 4.3 23.9 1.0 OD2 A:ASP274 4.4 17.9 1.0 O A:HOH2078 4.4 23.8 1.0 CG A:ASP274 4.5 19.3 1.0 O3B A:ADP1388 4.5 31.9 1.0 O A:HOH2129 4.6 9.8 1.0 CA A:GLY276 4.7 17.2 1.0 O A:HOH2021 4.9 35.2 1.0 CE A:LYS162 4.9 15.9 1.0 CD1 A:PHE144 5.0 20.3 1.0

Magnesium binding site 3 out of 3 in the Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Aurora-A 122-403, Phosphorylated on THR287, THR288 and Bound to TPX2 1-43 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1394 b:37.4 occ:1.00 O A:HOH2104 2.5 36.5 1.0 OE2 A:GLU308 3.8 41.5 1.0 O A:HOH2131 4.0 18.4 1.0 NH2 A:ARG251 4.3 32.0 1.0 O A:HIS248 4.3 16.4 1.0 OE1 A:GLU308 4.4 38.1 1.0 CD A:GLU308 4.5 33.6 1.0 O1 A:SO41391 4.7 40.6 1.0 C A:HIS248 4.7 16.0 1.0 O4 A:SO41391 4.7 46.5 1.0 CE A:MET373 4.8 34.4 1.0 CB A:HIS248 4.9 14.6 1.0 NE A:ARG251 5.0 31.2 1.0

R.Bayliss, T.Sardon, I.Vernos, E.Conti. Structural Basis of Aurora-A Activation By TPX2 at the Mitotic Spindle Mol.Cell V. 12 851 2003.
ISSN: ISSN 1097-2765
PubMed: 14580337
DOI: 10.1016/S1097-2765(03)00392-7