Manganese in PDB 3ng0: Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803

All present enzymatic activity of Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803:
6.3.1.2;

The structure of Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803, PDB code: 3ng0 was solved by L.Saelices, D.Cascio, F.J.Florencio, M.I.Muro-Pastor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.92 / 2.80
Space group	P 6 2 2
Cell size a, b, c (Å), α, β, γ (°)	132.016, 132.016, 202.130, 90.00, 90.00, 120.00
R / Rfree (%)	28.5 / 31.3

The binding sites of Manganese atom in the Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803 (pdb code 3ng0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803, PDB code: 3ng0:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn475 b:60.1 occ:1.00 OE1 A:GLU223 2.5 43.3 1.0 OE2 A:GLU134 2.6 43.3 1.0 OE2 A:GLU215 2.7 32.5 1.0 CD A:GLU215 3.4 34.7 1.0 CD A:GLU134 3.6 44.6 1.0 O2G A:ANP474 3.6 81.3 1.0 CD A:GLU223 3.7 49.6 1.0 CG A:GLU134 3.7 24.1 1.0 OE1 A:GLU215 3.9 34.2 1.0 NE2 A:HIS213 4.1 17.3 1.0 CG A:GLU215 4.2 20.8 1.0 CG A:GLU223 4.3 25.9 1.0 CD2 A:HIS272 4.5 34.7 1.0 NE2 A:HIS272 4.5 34.8 1.0 CE1 A:HIS213 4.6 17.1 1.0 OE1 A:GLU134 4.7 49.8 1.0 CB A:GLU223 4.7 14.4 1.0 OE2 A:GLU223 4.7 47.9 1.0 MN A:MN476 4.8 0.8 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn476 b:0.8 occ:1.00 O2G A:ANP474 2.6 81.3 1.0 N3B A:ANP474 3.0 36.2 1.0 PG A:ANP474 3.2 0.0 1.0 OE1 A:GLU132 3.4 57.6 1.0 O3G A:ANP474 3.5 0.7 1.0 O2A A:ANP474 3.7 82.2 1.0 CE1 A:HIS213 3.7 17.1 1.0 CE A:LYS211 3.7 38.4 1.0 OE1 A:GLU223 3.9 43.3 1.0 CD A:GLU132 4.1 50.7 1.0 OE2 A:GLU223 4.1 47.9 1.0 OE2 A:GLU132 4.2 37.6 1.0 CD A:GLU223 4.4 49.6 1.0 PB A:ANP474 4.5 52.1 1.0 ND1 A:HIS213 4.5 18.0 1.0 NE2 A:HIS213 4.6 17.3 1.0 O1G A:ANP474 4.7 34.5 1.0 NZ A:LYS211 4.7 54.2 1.0 O2B A:ANP474 4.7 0.2 1.0 PA A:ANP474 4.7 36.5 1.0 CD A:LYS211 4.8 19.8 1.0 MN A:MN475 4.8 60.1 1.0 O5' A:ANP474 4.8 0.9 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn477 b:78.3 occ:1.00 O1G A:ANP474 2.0 34.5 1.0 OE2 A:GLU361 2.1 21.2 1.0 OE2 A:GLU132 2.9 37.6 1.0 CG A:HIS272 3.0 31.5 1.0 CD A:GLU361 3.0 38.2 1.0 NH1 A:ARG363 3.1 39.5 1.0 CD2 A:HIS272 3.2 34.7 1.0 PG A:ANP474 3.2 0.0 1.0 O2G A:ANP474 3.3 81.3 1.0 CB A:HIS272 3.3 26.8 1.0 OE1 A:GLU361 3.5 28.0 1.0 ND1 A:HIS272 3.5 34.1 1.0 NE2 A:HIS272 3.7 34.8 1.0 CE1 A:HIS272 3.9 34.2 1.0 CZ A:ARG363 4.1 54.6 1.0 CD A:GLU132 4.2 50.7 1.0 CG A:GLU361 4.2 25.9 1.0 O3G A:ANP474 4.2 0.7 1.0 N3B A:ANP474 4.2 36.2 1.0 NE2 A:HIS274 4.4 24.1 1.0 O1B A:ANP474 4.4 42.0 1.0 NH2 A:ARG363 4.6 43.4 1.0 NH1 A:ARG347 4.6 49.5 1.0 CA A:HIS272 4.9 25.0 1.0 OE1 A:GLU132 4.9 57.6 1.0 PB A:ANP474 5.0 52.1 1.0

L.Saelices, D.Cascio, F.J.Florencio, M.I.Muro-Pastor. Crystal Structure of Glutamine Synthetase From Synechocystis Sp. Pcc 6803 To Be Published.