Magnesium in PDB 2dqn: Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Asn

The structure of Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Asn, PDB code: 2dqn 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 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.805, 92.363, 182.246, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 27.1

The binding sites of Magnesium atom in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Asn (pdb code 2dqn). 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 Asn, PDB code: 2dqn:

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


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 Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:33.5 occ:1.00 O B:HOH508 2.0 42.6 1.0 OE1 B:GLU150 2.2 39.9 1.0 NE2 B:HIS12 2.3 40.5 1.0 OE1 B:GLU124 2.4 36.8 1.0 OE2 B:GLU124 2.7 41.5 1.0 CD B:GLU124 2.9 40.0 1.0 CD B:GLU150 3.2 39.2 1.0 CE1 B:HIS12 3.2 39.8 1.0 CD2 B:HIS12 3.3 41.6 1.0 OE2 B:GLU150 3.9 44.1 1.0 CG B:GLU150 4.1 38.0 1.0 OE1 B:GLN91 4.1 31.9 1.0 O B:HOH530 4.2 35.3 1.0 NZ B:LYS79 4.2 47.5 1.0 ND1 B:HIS12 4.3 42.8 1.0 NE2 B:GLN91 4.3 31.9 1.0 CG B:GLU124 4.4 38.8 1.0 CG B:HIS12 4.4 44.1 1.0 CB B:GLU150 4.5 37.1 1.0 OE2 B:GLU10 4.6 55.4 1.0 CD B:GLN91 4.7 33.3 1.0 NE2 B:HIS122 4.8 25.4 1.0 CE B:LYS79 4.9 47.7 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