Calcium in PDB 4o2a: Tubulin-BAL27862 Complex

The structure of Tubulin-BAL27862 Complex, PDB code: 4o2a was solved by A.E.Prota, D.Franck, F.Bachmann, K.Bargsten, R.M.Buey, J.Pohlmann, S.Reinelt, H.Lane, M.O.Steinmetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.36 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	104.530, 158.120, 179.730, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.2

The structure of Tubulin-BAL27862 Complex also contains other interesting chemical elements:

Magnesium	(Mg)	5 atoms
Chlorine	(Cl)	1 atom

The binding sites of Calcium atom in the Tubulin-BAL27862 Complex (pdb code 4o2a). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Tubulin-BAL27862 Complex, PDB code: 4o2a:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Tubulin-BAL27862 Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Tubulin-BAL27862 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca503 b:62.2 occ:1.00 OD2 A:ASP39 2.5 59.9 1.0 OE2 A:GLU55 2.5 59.6 1.0 O A:GLY44 2.5 64.0 1.0 O A:THR41 2.5 70.6 1.0 OG1 A:THR41 2.5 73.4 1.0 OD1 A:ASP39 2.6 60.6 1.0 OE1 A:GLU55 2.8 76.5 1.0 CG A:ASP39 2.9 60.7 1.0 CD A:GLU55 3.0 68.6 1.0 C A:THR41 3.5 70.7 1.0 CB A:THR41 3.6 63.8 1.0 C A:GLY44 3.7 65.7 1.0 CA A:THR41 4.0 66.2 1.0 CZ A:PHE49 4.1 66.2 1.0 N A:THR41 4.2 67.9 1.0 OD2 A:ASP47 4.3 69.5 1.0 CB A:ASP39 4.4 59.8 1.0 CG A:GLU55 4.5 66.1 1.0 CA A:GLY45 4.5 69.3 1.0 OD1 A:ASN50 4.5 67.6 1.0 CE1 A:PHE49 4.5 65.7 1.0 N A:GLY45 4.5 66.5 1.0 NE2 A:HIS61 4.6 75.5 1.0 N A:GLY44 4.6 54.9 1.0 CA A:GLY44 4.7 61.1 1.0 N A:ILE42 4.7 69.7 1.0 ND2 A:ASN50 4.8 46.4 1.0 CG2 A:THR41 4.9 58.8 1.0

Calcium binding site 2 out of 4 in the Tubulin-BAL27862 Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Tubulin-BAL27862 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca503 b:81.7 occ:1.00 OE2 B:GLU113 2.8 60.5 1.0 CD B:GLU113 3.7 59.2 1.0 OE1 B:GLU113 3.8 70.3 1.0 OE1 B:GLU110 4.6 42.4 1.0

Calcium binding site 3 out of 4 in the Tubulin-BAL27862 Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Tubulin-BAL27862 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca502 b:58.9 occ:1.00 OG1 C:THR41 2.4 81.9 1.0 OD2 C:ASP39 2.4 59.7 1.0 OE2 C:GLU55 2.5 62.9 1.0 O C:GLY44 2.5 52.9 1.0 OE1 C:GLU55 2.5 49.3 1.0 O C:THR41 2.5 66.7 1.0 OD1 C:ASP39 2.6 59.1 1.0 CD C:GLU55 2.8 52.2 1.0 CG C:ASP39 2.9 60.5 1.0 CB C:THR41 3.6 73.9 1.0 C C:GLY44 3.6 56.1 1.0 C C:THR41 3.6 65.8 1.0 OD2 C:ASP47 3.9 65.0 1.0 CA C:THR41 4.0 66.0 1.0 O C:HOH628 4.0 31.0 1.0 CG C:GLU55 4.3 42.5 1.0 OD1 C:ASN50 4.3 44.1 1.0 N C:THR41 4.3 64.8 1.0 CB C:ASP39 4.4 60.4 1.0 CA C:GLY45 4.4 64.9 1.0 N C:GLY45 4.4 59.9 1.0 NE2 C:HIS61 4.5 43.0 1.0 CA C:GLY44 4.5 58.7 1.0 CZ C:PHE49 4.6 40.6 1.0 N C:GLY44 4.6 62.8 1.0 N C:ILE42 4.8 67.0 1.0 CG2 C:THR41 4.8 76.0 1.0 ND2 C:ASN50 4.9 33.5 1.0 CE1 C:PHE49 5.0 41.5 1.0

Calcium binding site 4 out of 4 in the Tubulin-BAL27862 Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Tubulin-BAL27862 Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca700 b:84.8 occ:1.00 O A:HOH650 2.7 63.0 1.0 O A:HOH651 2.9 56.8 1.0 OD2 E:ASP44 3.2 0.7 1.0 O A:HOH612 3.3 41.3 1.0 O A:HOH652 4.2 61.1 1.0 OG A:SER158 4.2 47.6 1.0 O A:GLY162 4.2 58.9 1.0 CG E:ASP44 4.3 0.6 1.0 NZ A:LYS166 4.5 45.7 1.0 CB A:SER158 4.5 33.7 1.0 O A:GLU196 4.6 46.1 1.0 OD1 E:ASP44 4.7 0.6 1.0

A.E.Prota, F.Danel, F.Bachmann, K.Bargsten, R.M.Buey, J.Pohlmann, S.Reinelt, H.Lane, M.O.Steinmetz. The Novel Microtubule-Destabilizing Drug BAL27862 Binds to the Colchicine Site of Tubulin with Distinct Effects on Microtubule Organization. J.Mol.Biol. V. 426 1848 2014.
ISSN: ISSN 0022-2836
PubMed: 24530796
DOI: 10.1016/J.JMB.2014.02.005