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Magnesium in PDB 8g97: Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound)

Protein crystallography data

The structure of Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound), PDB code: 8g97 was solved by K.D.Patel, A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.92 / 2.51
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.837, 93.928, 152.257, 90, 90, 90
R / Rfree (%) 19.4 / 24

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound) (pdb code 8g97). 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 Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound), PDB code: 8g97:

Magnesium binding site 1 out of 1 in 8g97

Go back to Magnesium Binding Sites List in 8g97
Magnesium binding site 1 out of 1 in the Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Adenylation Domain Structure From Nrps-Like Delta-Poly-L-Ornithine Synthetase (D-Ornithine Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg506

b:93.3
occ:1.00
O A:HOH606 3.2 70.4 1.0
N A:THR308 3.4 54.8 1.0
OE1 A:GLU309 3.4 63.5 1.0
CA A:PRO307 3.9 57.8 1.0
O A:ORD507 3.9 98.6 1.0
OG1 A:THR308 4.0 59.7 1.0
CB A:PRO307 4.0 57.6 1.0
CB A:THR308 4.1 57.6 1.0
C A:PRO307 4.2 54.6 1.0
CD A:GLU309 4.3 62.4 1.0
OE2 A:GLU309 4.3 62.1 1.0
CA A:THR308 4.4 52.5 1.0
N A:GLU309 5.0 50.4 1.0

Reference:

K.D.Patel, A.M.Gulick. Structural and Functional Insights Into Delta-Poly-L-Ornithine Polymer Biosynthesis From Acinetobacter Baumannii Commun Biol V. 6 982 2023.
ISSN: ESSN 2399-3642
DOI: 10.1038/S42003-023-05362-4
Page generated: Thu Dec 28 09:06:09 2023

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