Magnesium in PDB 5dmz: Structure of Human BUB1 Kinase Domain Phosphorylated at SER969

All present enzymatic activity of Structure of Human BUB1 Kinase Domain Phosphorylated at SER969:
2.7.11.1;

The structure of Structure of Human BUB1 Kinase Domain Phosphorylated at SER969, PDB code: 5dmz was solved by C.Breit, J.R.Weir, A.Musacchio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.30 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.380, 66.340, 106.540, 90.00, 98.34, 90.00
R / Rfree (%)	21.1 / 24.5

The binding sites of Magnesium atom in the Structure of Human BUB1 Kinase Domain Phosphorylated at SER969 (pdb code 5dmz). 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 Human BUB1 Kinase Domain Phosphorylated at SER969, PDB code: 5dmz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human BUB1 Kinase Domain Phosphorylated at SER969


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human BUB1 Kinase Domain Phosphorylated at SER969 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1102 b:57.1 occ:1.00 O A:HOH1210 2.0 51.8 1.0 OD2 A:ASP946 2.1 66.8 1.0 O3B A:ADP1101 2.1 50.7 1.0 O A:HOH1209 2.1 48.7 1.0 O1A A:ADP1101 2.1 48.1 1.0 OD1 A:ASN922 2.2 56.1 1.0 CG A:ASP946 3.2 67.7 1.0 H5'2 A:ADP1101 3.2 73.8 1.0 CG A:ASN922 3.2 59.4 1.0 PB A:ADP1101 3.3 54.0 1.0 HB2 A:ASP946 3.4 83.2 1.0 PA A:ADP1101 3.5 52.6 1.0 ND2 A:ASN922 3.5 60.1 1.0 O1B A:ADP1101 3.7 53.4 1.0 CB A:ASP946 3.8 69.3 1.0 O3A A:ADP1101 3.8 1.0 1.0 HB3 A:ASP946 4.0 83.2 1.0 C5' A:ADP1101 4.1 61.5 1.0 OD1 A:ASP946 4.2 67.7 1.0 HB2 A:ASP921 4.2 76.7 1.0 H5'1 A:ADP1101 4.3 73.8 1.0 O5' A:ADP1101 4.3 56.6 1.0 HA3 A:GLY796 4.3 90.0 1.0 OD2 A:ASP917 4.3 90.5 1.0 HB3 A:ASP921 4.5 76.7 1.0 HA A:ASN922 4.5 72.0 1.0 O2B A:ADP1101 4.6 58.7 1.0 CB A:ASN922 4.6 57.7 1.0 O2A A:ADP1101 4.6 59.5 1.0 HZ3 A:LYS919 4.6 94.0 1.0 H3' A:ADP1101 4.7 83.8 1.0 CB A:ASP921 4.8 63.9 1.0 CA A:ASN922 4.9 60.0 1.0 HD3 A:LYS919 5.0 87.4 1.0 O2P A:SEP969 5.0 93.2 1.0 O A:ASP921 5.0 65.0 1.0

Magnesium binding site 2 out of 2 in the Structure of Human BUB1 Kinase Domain Phosphorylated at SER969


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human BUB1 Kinase Domain Phosphorylated at SER969 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1102 b:53.4 occ:1.00 O2A B:ADP1101 1.9 52.6 1.0 OD2 B:ASP946 2.0 69.3 1.0 O1B B:ADP1101 2.0 53.6 1.0 O B:HOH1202 2.1 52.0 1.0 O B:HOH1205 2.3 48.8 1.0 OD1 B:ASN922 2.4 59.9 1.0 HD21 B:ASN922 3.1 69.8 1.0 CG B:ASP946 3.1 69.6 1.0 PB B:ADP1101 3.1 52.3 1.0 PA B:ADP1101 3.2 51.2 1.0 H5'2 B:ADP1101 3.3 74.9 1.0 CG B:ASN922 3.3 60.3 1.0 HB2 B:ASP946 3.5 85.2 1.0 O3B B:ADP1101 3.5 55.0 1.0 ND2 B:ASN922 3.5 58.2 1.0 O3A B:ADP1101 3.6 0.1 1.0 CB B:ASP946 3.8 71.0 1.0 OD1 B:ASP946 4.0 68.6 1.0 HB3 B:ASP946 4.1 85.2 1.0 OD2 B:ASP917 4.1 85.7 1.0 HZ3 B:LYS919 4.1 93.7 1.0 C5' B:ADP1101 4.2 62.4 1.0 O5' B:ADP1101 4.2 57.8 1.0 O1A B:ADP1101 4.3 58.5 1.0 HA3 B:GLY796 4.3 80.5 1.0 HD22 B:ASN922 4.4 69.8 1.0 OD2 B:ASP921 4.4 64.9 0.3 O2B B:ADP1101 4.5 61.1 1.0 H3' B:ADP1101 4.6 78.9 1.0 HA B:ASN922 4.7 65.6 1.0 HE3 B:LYS919 4.7 90.3 1.0 H5'1 B:ADP1101 4.7 74.9 1.0 CB B:ASN922 4.8 55.7 1.0 O2P B:SEP969 4.8 81.9 1.0 HZ2 B:LYS821 4.9 78.9 1.0 O B:ASP921 4.9 63.0 1.0 NZ B:LYS919 4.9 78.1 1.0 HA2 B:GLY796 4.9 80.5 1.0

C.Breit, T.Bange, A.Petrovic, J.R.Weir, F.Muller, D.Vogt, A.Musacchio. Role of Intrinsic and Extrinsic Factors in the Regulation of the Mitotic Checkpoint Kinase BUB1. Plos One V. 10 44673 2015.
ISSN: ESSN 1932-6203
PubMed: 26658523
DOI: 10.1371/JOURNAL.PONE.0144673