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Magnesium in PDB 2g5i: Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Adp-ALF4

Protein crystallography data

The structure of Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Adp-ALF4, PDB code: 2g5i 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 / 3.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.860, 85.279, 183.625, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 29.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Adp-ALF4 (pdb code 2g5i). 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 Adp-ALF4, PDB code: 2g5i:

Magnesium binding site 1 out of 1 in 2g5i

Go back to Magnesium Binding Sites List in 2g5i
Magnesium binding site 1 out of 1 in the Structure of Trna-Dependent Amidotransferase Gatcab Complexed with Adp-ALF4


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 Adp-ALF4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:24.0
occ:1.00
OE2 B:GLU150 1.7 24.2 1.0
NE2 B:HIS12 2.4 24.0 1.0
O B:HOH603 2.6 24.0 1.0
OE1 B:GLU124 2.7 27.9 1.0
OE2 B:GLU124 2.8 25.1 1.0
CD B:GLU150 2.9 24.0 1.0
CD B:GLU124 3.1 26.1 1.0
CE1 B:HIS12 3.2 24.1 1.0
CD2 B:HIS12 3.6 24.0 1.0
OE1 B:GLU150 3.8 24.0 1.0
CG B:GLU150 3.8 24.0 1.0
ND1 B:HIS12 4.4 26.0 1.0
CG B:GLU124 4.6 24.0 1.0
CG B:HIS12 4.6 24.0 1.0
OE2 B:GLU10 4.9 43.5 1.0
CE B:LYS79 4.9 24.0 1.0
NE2 B:HIS122 4.9 24.0 1.0
OE1 B:GLN91 4.9 24.0 1.0
CB B:GLU150 4.9 24.0 1.0

Reference:

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
Page generated: Tue Aug 13 23:23:16 2024

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