Magnesium in PDB 8v31: Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2

The structure of Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2, PDB code: 8v31 was solved by A.C.Lazarski, L.J.Worrall, N.C.J.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.54 / 2.65
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.088, 95.088, 159.542, 90, 90, 120
R / Rfree (%)	19.7 / 24.4

The binding sites of Magnesium atom in the Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2 (pdb code 8v31). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2, PDB code: 8v31:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:50.5 occ:1.00 OE1 A:GLN166 2.1 69.0 1.0 OE1 A:GLU164 2.3 56.5 1.0 OE1 A:GLN273 2.4 46.6 1.0 OD1 A:ASN135 2.5 62.5 1.0 O A:HOH417 2.7 58.6 1.0 O A:SER136 2.7 59.0 1.0 CD A:GLN166 3.3 66.3 1.0 CD A:GLN273 3.4 47.2 1.0 CD A:GLU164 3.5 53.9 1.0 C A:SER136 3.5 49.1 1.0 CG A:ASN135 3.7 63.4 1.0 NE2 A:GLN273 3.8 58.2 1.0 NE2 A:GLN166 3.9 77.2 1.0 OE2 A:GLU164 4.0 61.0 1.0 ND2 A:ASN135 4.2 79.6 1.0 CA A:SER136 4.3 59.7 1.0 N A:SER136 4.3 59.6 1.0 N A:GLY137 4.3 53.6 1.0 CG A:GLN166 4.5 66.5 1.0 CA A:GLY137 4.5 67.3 1.0 CD2 A:HIS275 4.5 63.2 1.0 O A:VAL167 4.7 49.5 1.0 CA A:GLN166 4.8 60.3 1.0 CG A:GLU164 4.8 51.5 1.0 CG A:GLN273 4.8 52.2 1.0 N A:VAL167 4.8 50.2 1.0 CB A:GLN166 4.9 64.7 1.0 CB A:ASN135 4.9 63.0 1.0 C A:ASN135 4.9 62.4 1.0 CG A:HIS275 4.9 66.8 1.0 CD2 A:TYR190 5.0 50.7 1.0 NE2 A:HIS275 5.0 59.2 1.0

Magnesium binding site 2 out of 2 in the Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Alistipes Sp. 3-Keto-2-Hydroxy-Glucal-Hydratase AL2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg301 b:35.0 occ:1.00 OE1 C:GLN166 2.2 57.1 1.0 OE1 C:GLN273 2.2 60.8 1.0 OD1 C:ASN135 2.2 46.6 1.0 OE1 C:GLU164 2.4 50.8 1.0 O C:SER136 2.5 41.4 1.0 O C:HOH412 2.8 31.7 1.0 O C:HOH408 2.9 36.9 1.0 C C:SER136 3.2 41.7 1.0 CD C:GLN273 3.4 41.5 1.0 CD C:GLN166 3.4 57.8 1.0 CG C:ASN135 3.4 48.7 1.0 CD C:GLU164 3.6 48.0 1.0 ND2 C:ASN135 3.9 60.0 1.0 CA C:SER136 4.0 43.8 1.0 NE2 C:GLN166 4.0 50.4 1.0 NE2 C:GLN273 4.0 45.8 1.0 N C:SER136 4.0 46.6 1.0 N C:GLY137 4.1 48.0 1.0 OE2 C:GLU164 4.1 55.2 1.0 CD2 C:HIS275 4.2 62.0 1.0 CA C:GLY137 4.4 50.1 1.0 O C:VAL167 4.4 39.8 1.0 CG C:GLN273 4.6 37.9 1.0 CG C:GLN166 4.6 42.6 1.0 CG C:HIS275 4.7 54.6 1.0 C C:ASN135 4.7 56.4 1.0 CB C:ASN135 4.7 53.5 1.0 NE2 C:HIS275 4.8 55.6 1.0 N C:VAL167 4.8 42.0 1.0 CG C:GLU164 4.8 55.5 1.0 CA C:GLN166 4.8 44.2 1.0 CB C:HIS275 5.0 40.0 1.0

S.A.Nasseri, A.C.Lazarski, I.L.Lemmer, C.Y.Zhang, E.Brencher, H.Chen, L.Sim, D.Panwar, L.Betschart, L.J.Worrall, H.Brumer, N.C.J.Strynadka, S.G.Withers. An Alternative Broad-Specificity Pathway For Glycan Breakdown in Bacteria To Be Published.