Magnesium in PDB 1i7q: Anthranilate Synthase From S. Marcescens

All present enzymatic activity of Anthranilate Synthase From S. Marcescens:
4.1.3.27;

The structure of Anthranilate Synthase From S. Marcescens, PDB code: 1i7q was solved by G.Spraggon, C.Kim, X.Nguyen-Huu, M.-C.Yee, C.Yanofsky, S.E.Mills, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.50 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.316, 68.984, 116.363, 90.00, 108.52, 90.00
R / Rfree (%)	18.1 / 24.6

The binding sites of Magnesium atom in the Anthranilate Synthase From S. Marcescens (pdb code 1i7q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Anthranilate Synthase From S. Marcescens, PDB code: 1i7q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Anthranilate Synthase From S. Marcescens


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Anthranilate Synthase From S. Marcescens within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1701 b:20.1 occ:1.00 O A:HOH1760 2.2 10.0 1.0 O2 A:BEZ1501 2.3 13.1 1.0 O A:HOH1898 2.4 12.8 1.0 OE2 A:GLU498 2.4 17.3 1.0 O1 A:BEZ1501 2.5 16.0 1.0 C A:BEZ1501 2.8 16.5 1.0 OE2 A:GLU361 2.8 15.6 1.0 CD A:GLU498 3.2 21.3 1.0 OE1 A:GLU498 3.3 22.6 1.0 CD A:GLU361 3.7 21.9 1.0 OE1 A:GLU361 3.8 15.1 1.0 N A:THR329 4.0 14.1 1.0 OG1 A:THR329 4.0 11.1 1.0 OE1 A:GLU358 4.1 41.3 1.0 N A:GLY328 4.1 13.4 1.0 NZ A:LYS357 4.1 13.8 1.0 CA A:GLY328 4.2 12.5 1.0 N A:GLY485 4.2 12.8 1.0 C1 A:BEZ1501 4.3 18.6 1.0 O A:HOH1812 4.3 29.5 1.0 CB A:THR329 4.3 11.6 1.0 NZ A:LYS502 4.3 16.5 1.0 C A:GLY328 4.4 13.6 1.0 OE2 A:GLU495 4.4 13.4 1.0 O A:GLY485 4.6 17.2 1.0 O A:HOH1715 4.6 10.3 1.0 CG A:GLU498 4.7 19.9 1.0 CA A:THR329 4.7 8.1 1.0 CA A:GLY485 4.8 10.3 1.0 CB A:ALA484 4.8 13.0 1.0 OE2 A:GLU358 4.9 27.4 1.0 CD A:GLU358 4.9 31.8 1.0

Magnesium binding site 2 out of 2 in the Anthranilate Synthase From S. Marcescens


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Anthranilate Synthase From S. Marcescens within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1702 b:27.3 occ:1.00 O1 C:BEZ1502 2.2 24.2 1.0 O2 C:BEZ1502 2.3 18.9 1.0 O C:HOH1719 2.4 17.9 1.0 O C:HOH1716 2.6 18.6 1.0 OE2 C:GLU498 2.6 24.1 1.0 C C:BEZ1502 2.6 30.5 1.0 OE2 C:GLU361 2.6 27.9 1.0 CD C:GLU498 3.4 28.1 1.0 OE1 C:GLU498 3.4 24.8 1.0 CD C:GLU361 3.6 30.1 1.0 OE1 C:GLU361 3.7 22.7 1.0 N C:GLY485 4.0 26.2 1.0 N C:GLY328 4.1 14.8 1.0 OG1 C:THR329 4.1 17.8 1.0 C1 C:BEZ1502 4.1 29.8 1.0 NZ C:LYS357 4.2 15.8 1.0 N C:THR329 4.2 13.5 1.0 O C:HOH1768 4.2 18.3 1.0 NZ C:LYS502 4.3 22.8 1.0 CA C:GLY328 4.3 13.3 1.0 O C:GLY485 4.5 18.9 1.0 CB C:THR329 4.5 13.2 1.0 CA C:GLY485 4.5 20.1 1.0 C C:GLY328 4.6 15.1 1.0 O C:HOH1888 4.6 34.2 1.0 OE2 C:GLU495 4.6 30.1 1.0 CG C:GLU498 4.8 20.5 1.0 CB C:ALA484 4.8 30.2 1.0 CA C:ALA484 4.9 23.4 1.0 C C:ALA484 4.9 25.5 1.0 C2 C:BEZ1502 5.0 31.5 1.0 C C:GLY485 5.0 24.9 1.0

G.Spraggon, C.Kim, X.Nguyen-Huu, M.C.Yee, C.Yanofsky, S.E.Mills. The Structures of Anthranilate Synthase of Serratia Marcescens Crystallized in the Presence of (I) Its Substrates, Chorismate and Glutamine, and A Product, Glutamate, and (II) Its End-Product Inhibitor, L-Tryptophan. Proc.Natl.Acad.Sci.Usa V. 98 6021 2001.
ISSN: ISSN 0027-8424
PubMed: 11371633
DOI: 10.1073/PNAS.111150298