Magnesium in PDB 6jkm: Crystal Structure of BUBR1 Kinase Domain

The structure of Crystal Structure of BUBR1 Kinase Domain, PDB code: 6jkm was solved by L.Lin, S.Ye, Y.Huang, X.Liu, R.Zhang, X.Yao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.37 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.333, 61.979, 96.232, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22.6

The binding sites of Magnesium atom in the Crystal Structure of BUBR1 Kinase Domain (pdb code 6jkm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of BUBR1 Kinase Domain, PDB code: 6jkm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of BUBR1 Kinase Domain


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 BUBR1 Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1502 b:21.6 occ:1.00 O A:HOH1701 1.9 22.6 1.0 O2A A:ADP1501 2.0 20.4 1.0 O A:HOH1683 2.1 22.3 1.0 OD1 A:ASN1306 2.1 14.9 1.0 O3B A:ADP1501 2.2 22.0 1.0 OD1 A:ASP1326 2.2 18.0 1.0 CG A:ASN1306 3.1 14.9 1.0 CG A:ASP1326 3.1 17.6 1.0 PA A:ADP1501 3.3 20.4 1.0 PB A:ADP1501 3.3 22.1 1.0 ND2 A:ASN1306 3.5 14.6 1.0 CB A:ASP1326 3.5 16.6 1.0 O3A A:ADP1501 3.6 21.0 1.0 O2B A:ADP1501 3.8 21.8 1.0 O A:HOH1783 3.9 23.9 1.0 MG A:MG1503 4.0 26.1 1.0 OD2 A:ASP1326 4.2 18.1 1.0 O5' A:ADP1501 4.2 16.1 1.0 C5' A:ADP1501 4.3 16.0 1.0 O1A A:ADP1501 4.4 20.4 1.0 O A:HOH1743 4.4 33.6 1.0 CB A:ASN1306 4.5 14.5 1.0 O1B A:ADP1501 4.6 21.9 1.0 O3' A:ADP1501 4.6 16.0 1.0 OD2 A:ASP1301 4.8 22.8 1.0 CB A:ASP1305 4.8 22.3 1.0 O A:ASP1305 4.8 15.2 1.0 CA A:ASN1306 4.9 14.0 1.0 O A:HOH1845 4.9 39.5 1.0 C A:ASP1305 5.0 15.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of BUBR1 Kinase Domain


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 BUBR1 Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1503 b:26.1 occ:1.00 O A:HOH1805 1.9 39.6 1.0 O A:HOH1783 1.9 23.9 1.0 O2B A:ADP1501 2.1 21.8 1.0 OD2 A:ASP1326 2.2 18.1 1.0 OD1 A:ASP1326 2.3 18.0 1.0 CG A:ASP1326 2.6 17.6 1.0 O A:HOH1659 2.8 27.2 1.0 PB A:ADP1501 3.3 22.1 1.0 O A:HOH1689 3.3 27.5 1.0 O3B A:ADP1501 3.5 22.0 1.0 MG A:MG1502 4.0 21.6 1.0 O A:HOH1701 4.1 22.6 1.0 CB A:ASP1326 4.1 16.6 1.0 NZ A:LYS1204 4.1 15.8 1.0 OD2 A:ASP1301 4.2 22.8 1.0 O1B A:ADP1501 4.3 21.9 1.0 O3A A:ADP1501 4.4 21.0 1.0 O2A A:ADP1501 4.8 20.4 1.0 CA A:GLY1328 4.8 19.4 1.0 N A:GLY1328 4.8 18.8 1.0 O A:ASP1326 4.9 16.1 1.0 CA A:ASP1326 4.9 16.0 1.0 O A:HOH1762 4.9 55.6 1.0 O A:HOH1691 5.0 54.0 1.0

Y.Huang, L.Lin, X.Liu, S.Ye, P.Y.Yao, W.Wang, F.Yang, X.Gao, J.Li, Y.Zhang, J.Zhang, Z.Yang, X.Liu, Z.Yang, J.Zang, M.Teng, Z.Wang, K.Ruan, X.Ding, L.Li, D.W.Cleveland, R.Zhang, X.Yao. BUBR1 Phosphorylates Cenp-E As A Switch Enabling the Transition From Lateral Association to End-on Capture of Spindle Microtubules. Cell Res. V. 29 562 2019.
ISSN: ISSN 1001-0602
PubMed: 31201382
DOI: 10.1038/S41422-019-0178-Z