Magnesium in PDB 7nsf: Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium

The structure of Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium, PDB code: 7nsf was solved by M.S.Vogt, L.-O.Essen, A.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.15 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.029, 61.029, 136.619, 90, 90, 90
R / Rfree (%)	20.7 / 23.9

The binding sites of Magnesium atom in the Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium (pdb code 7nsf). 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 Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium, PDB code: 7nsf:

Magnesium binding site 1 out of 1 in the Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Triphosphate Tunnel Metalloenzyme From Sulfolobus Acidocaldarius in Complex with Triphosphate and Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:56.9 occ:1.00 O3G A:3PO201 2.1 57.4 0.8 O5' A:3PO201 2.2 41.9 1.0 OE2 A:GLU7 2.2 74.9 1.0 OE1 A:GLU135 2.2 48.2 1.0 O1B A:3PO201 2.3 54.8 1.0 OE2 A:GLU135 2.3 59.2 1.0 CD A:GLU135 2.6 53.7 1.0 CD A:GLU7 2.9 61.5 1.0 HZ1 A:LYS78 2.9 89.0 1.0 OE1 A:GLU7 3.1 74.2 1.0 O A:HOH317 3.2 73.8 1.0 PB A:3PO201 3.3 52.4 1.0 PG A:3PO201 3.4 86.8 0.8 HZ1 A:LYS9 3.4 75.2 1.0 PA A:3PO201 3.4 50.6 1.0 HH22 A:ARG112 3.6 49.4 1.0 O3B A:3PO201 3.6 60.4 1.0 NZ A:LYS78 3.8 74.1 1.0 O3A A:3PO201 3.8 59.9 1.0 HZ3 A:LYS9 4.0 75.2 1.0 CG A:GLU135 4.0 44.3 1.0 HE2 A:LYS78 4.1 80.2 1.0 HZ2 A:LYS78 4.1 89.0 1.0 O2A A:3PO201 4.1 54.8 1.0 NZ A:LYS9 4.1 62.6 1.0 HZ1 A:LYS69 4.2 70.5 1.0 HE3 A:LYS78 4.2 80.2 1.0 CG A:GLU7 4.2 51.0 1.0 HG3 A:GLU7 4.2 61.4 1.0 NH2 A:ARG112 4.2 41.1 1.0 CE A:LYS78 4.3 66.8 1.0 HE2 A:TYR168 4.3 52.9 1.0 OE1 A:GLU5 4.3 88.5 1.0 HB3 A:GLU135 4.3 49.6 1.0 O2G A:3PO201 4.3 52.1 0.8 HG2 A:GLU135 4.3 53.3 1.0 HZ3 A:LYS78 4.4 89.0 1.0 O1G A:3PO201 4.4 82.3 0.8 HZ3 A:LYS69 4.4 70.5 1.0 O A:HOH353 4.4 67.4 1.0 HH12 A:ARG112 4.5 58.4 1.0 HG3 A:GLU135 4.6 53.3 1.0 HH21 A:ARG112 4.6 49.4 1.0 OE2 A:GLU5 4.6 88.0 1.0 HZ2 A:LYS9 4.6 75.2 1.0 O1A A:3PO201 4.6 59.8 1.0 HG2 A:GLU7 4.6 61.4 1.0 O2B A:3PO201 4.7 45.2 1.0 NZ A:LYS69 4.7 58.7 1.0 CB A:GLU135 4.7 41.2 1.0 CD A:GLU5 4.7 94.8 1.0 CE2 A:TYR168 4.9 44.0 1.0 HZ2 A:LYS69 4.9 70.5 1.0 HE2 A:LYS9 5.0 80.0 1.0 HB2 A:GLU135 5.0 49.6 1.0

M.S.Vogt, R.R.Ngouoko Nguepbeu, M.K.F.Mohr, S.V.Albers, L.O.Essen, A.Banerjee. The Archaeal Triphosphate Tunnel Metalloenzyme Sattm Defines Structural Determinants For the Diverse Activities in the Cyth Protein Family. J.Biol.Chem. 00820 2021.
ISSN: ESSN 1083-351X
PubMed: 34029589
DOI: 10.1016/J.JBC.2021.100820