Magnesium in PDB 4h2y: Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp

The structure of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp, PDB code: 4h2y was solved by M.Luic, I.Weygand-Durasevic, N.Ivic, M.Mocibob, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.08 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	99.863, 101.587, 103.424, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21

The structure of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp (pdb code 4h2y). 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 Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp, PDB code: 4h2y:

Magnesium binding site 1 out of 1 in the Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:51.7 occ:1.00 O1B A:ATP402 2.2 46.0 0.9 OE2 A:GLU237 2.5 37.4 1.0 O2A A:ATP402 2.9 53.4 0.9 PB A:ATP402 3.2 64.0 0.9 CD A:GLU237 3.3 30.1 1.0 CB A:ALA250 3.3 18.7 1.0 O2B A:ATP402 3.5 53.9 0.9 C3' A:ATP402 3.6 37.3 0.9 CG A:GLU237 3.6 29.6 1.0 O3' A:ATP402 3.7 39.2 0.9 O3A A:ATP402 3.7 57.2 0.9 PA A:ATP402 3.8 51.2 0.9 CE A:LYS235 3.9 38.6 1.0 NZ A:LYS235 4.0 39.1 1.0 CB A:SER253 4.0 23.1 1.0 O5' A:ATP402 4.2 37.1 0.9 OG A:SER253 4.2 31.9 1.0 OE1 A:GLU237 4.3 42.1 1.0 O3B A:ATP402 4.4 58.6 0.9 C2' A:ATP402 4.5 23.6 0.9 CA A:ALA250 4.7 22.5 1.0 CB A:GLU237 4.7 19.6 1.0 C4' A:ATP402 4.7 35.2 0.9 O A:ALA250 4.8 21.0 1.0 C5' A:ATP402 4.8 38.1 0.9 C A:ALA250 4.9 22.4 1.0 NH1 A:ARG286 4.9 20.8 1.0 O A:MET252 5.0 20.7 1.0

M.Mocibob, N.Ivic, M.Luic, I.Weygand-Durasevic. Adaptation of Aminoacyl-Trna Synthetase Catalytic Core to Carrier Protein Aminoacylation. Structure V. 21 614 2013.
ISSN: ISSN 0969-2126
PubMed: 23541895
DOI: 10.1016/J.STR.2013.02.017