Magnesium in PDB 2f2a: Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln

The structure of Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln, PDB code: 2f2a was solved by A.Nakamura, M.Yao, I.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	77.187, 88.222, 183.401, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 25.2

The binding sites of Magnesium atom in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln (pdb code 2f2a). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln, PDB code: 2f2a:

Magnesium binding site 1 out of 1 in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Gln within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:52.0 occ:1.00 OE2 B:GLU124 2.0 38.8 1.0 OE1 B:GLU150 2.1 40.5 1.0 NE2 B:HIS12 2.1 48.1 1.0 O B:HOH637 2.3 46.6 1.0 O B:HOH636 2.3 50.6 1.0 O B:HOH638 2.4 55.9 1.0 CD B:GLU124 3.0 36.4 1.0 CE1 B:HIS12 3.0 46.4 1.0 CD2 B:HIS12 3.2 46.5 1.0 CD B:GLU150 3.3 42.6 1.0 OE1 B:GLU124 3.3 34.1 1.0 CG B:GLU150 4.0 40.5 1.0 O B:HOH635 4.1 48.6 1.0 ND1 B:HIS12 4.2 45.9 1.0 OE2 B:GLU150 4.2 42.6 1.0 O B:HOH640 4.2 55.0 1.0 CG B:HIS12 4.3 46.0 1.0 OE1 B:GLN91 4.3 40.1 1.0 CG B:GLU124 4.4 35.5 1.0 CB B:GLU150 4.4 39.3 1.0 NE2 B:GLN91 4.4 35.8 1.0 NZ B:LYS79 4.6 36.4 1.0 NE2 B:HIS122 4.6 39.2 1.0 CD B:GLN91 4.8 37.1 1.0 O B:HOH691 5.0 60.3 1.0

A.Nakamura, M.Yao, S.Chimnaronk, N.Sakai, I.Tanaka. Ammonia Channel Couples Glutaminase with Transamidase Reactions in Gatcab Science V. 312 1954 2006.
ISSN: ISSN 0036-8075
PubMed: 16809541
DOI: 10.1126/SCIENCE.1127156