Magnesium in PDB 3tig: Tubulin Tyrosine Ligase

The structure of Tubulin Tyrosine Ligase, PDB code: 3tig was solved by A.Roll-Mecak, A.Szyk, A.Deaconescu, G.Piszczek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.24 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.570, 76.220, 44.240, 90.00, 90.64, 90.00
R / Rfree (%)	25 / 29.8

The binding sites of Magnesium atom in the Tubulin Tyrosine Ligase (pdb code 3tig). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Tubulin Tyrosine Ligase, PDB code: 3tig:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Tubulin Tyrosine Ligase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tubulin Tyrosine Ligase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg378 b:44.3 occ:1.00 OH A:TYR14 2.6 44.3 1.0 N A:LEU314 2.8 37.0 1.0 O A:ASN63 2.9 43.2 1.0 CA A:GLN313 3.4 34.1 1.0 CG A:GLN313 3.5 29.5 1.0 CZ A:TYR14 3.5 44.4 1.0 C A:GLN313 3.6 36.9 1.0 CB A:LEU314 3.6 38.0 1.0 CE2 A:TYR14 3.7 43.3 1.0 CA A:LEU314 3.7 37.6 1.0 O A:LEU314 3.9 39.2 1.0 CB A:GLN313 4.0 31.2 1.0 C A:ASN63 4.0 40.7 1.0 C A:LEU314 4.3 37.9 1.0 CB A:ASN63 4.3 36.7 1.0 CE1 A:TYR64 4.4 48.6 1.0 CZ A:TYR64 4.6 49.6 1.0 O A:GLY334 4.6 45.4 1.0 N A:GLN313 4.6 33.5 1.0 O A:PHE312 4.6 30.9 1.0 CD A:GLN313 4.6 30.6 1.0 ND2 A:ASN63 4.7 41.0 1.0 CD1 A:TYR64 4.7 46.1 1.0 CG A:ASN63 4.7 40.3 1.0 CA A:ASN63 4.7 39.2 1.0 O A:GLN313 4.8 36.3 1.0 CE1 A:TYR14 4.8 44.3 1.0 CE1 A:PHE312 4.8 31.6 1.0 OH A:TYR64 4.9 52.1 1.0 CE2 A:TYR64 4.9 48.2 1.0 CD1 A:PHE312 4.9 28.1 1.0 CD2 A:TYR14 5.0 43.2 1.0 C A:PHE312 5.0 34.0 1.0

Magnesium binding site 2 out of 2 in the Tubulin Tyrosine Ligase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Tubulin Tyrosine Ligase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg379 b:58.0 occ:1.00 ND2 A:ASN63 2.5 41.0 1.0 O A:GLY42 2.6 58.7 1.0 C A:LEU41 3.3 49.3 1.0 N A:GLY42 3.5 51.7 1.0 O A:LEU41 3.5 49.4 1.0 CG A:ASN63 3.5 40.3 1.0 CD2 A:TYR14 3.6 43.2 1.0 CA A:LEU41 3.6 46.6 1.0 C A:GLY42 3.7 58.3 1.0 CB A:LEU41 3.7 44.2 1.0 CG A:TYR14 3.7 47.1 1.0 OD1 A:ASN63 3.7 39.5 1.0 CB A:ASP8 3.8 69.6 1.0 CE2 A:TYR64 3.9 48.2 1.0 CB A:TYR14 3.9 48.1 1.0 CA A:GLY42 4.1 55.0 1.0 CE2 A:TYR14 4.3 43.3 1.0 CD1 A:TYR14 4.5 44.2 1.0 OH A:TYR64 4.5 52.1 1.0 OD2 A:ASP8 4.5 71.3 1.0 CG A:ASP8 4.6 70.3 1.0 CZ A:TYR64 4.6 49.6 1.0 CD2 A:TYR64 4.7 45.7 1.0 CB A:SER11 4.8 59.9 1.0 OG A:SER11 4.8 54.5 1.0 N A:GLU43 4.8 61.4 1.0 CB A:ASN63 4.9 36.7 1.0 CG A:LEU41 4.9 43.6 1.0 CZ A:TYR14 5.0 44.4 1.0

A.Szyk, A.M.Deaconescu, G.Piszczek, A.Roll-Mecak. Tubulin Tyrosine Ligase Structure Reveals Adaptation of An Ancient Fold to Bind and Modify Tubulin. Nat.Struct.Mol.Biol. V. 18 1250 2011.
ISSN: ISSN 1545-9993
PubMed: 22020298
DOI: 10.1038/NSMB.2148