Magnesium in PDB 5ji2: Hslu L199Q in Hsluv Complex

All present enzymatic activity of Hslu L199Q in Hsluv Complex:
3.4.25.2;

The structure of Hslu L199Q in Hsluv Complex, PDB code: 5ji2 was solved by R.A.Grant, R.T.Sauer, K.R.Schmitz, V.Baytshtok, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.08 / 3.31
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	170.005, 170.005, 163.385, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 28.1

The binding sites of Magnesium atom in the Hslu L199Q in Hsluv Complex (pdb code 5ji2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Hslu L199Q in Hsluv Complex, PDB code: 5ji2:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Hslu L199Q in Hsluv Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hslu L199Q in Hsluv Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:62.1 occ:1.00 O A:THR162 2.6 0.6 1.0 HA A:ILE160 2.7 0.8 1.0 O A:CYS159 2.8 0.1 1.0 O A:GLY156 3.0 0.1 1.0 O A:ILE160 3.3 0.4 1.0 CA A:ILE160 3.5 0.3 1.0 C A:ILE160 3.5 0.4 1.0 H A:THR162 3.7 0.1 1.0 C A:THR162 3.7 0.8 1.0 C A:CYS159 3.8 0.2 1.0 HA A:ASN163 4.0 0.4 1.0 OE1 A:GLN19 4.0 0.1 1.0 N A:ILE160 4.1 0.8 1.0 C A:GLY156 4.2 0.1 1.0 N A:THR162 4.2 0.7 1.0 HE22 A:GLN19 4.3 0.6 1.0 HA2 A:GLY156 4.4 0.8 1.0 N A:TYR161 4.5 0.0 1.0 HG22 A:ILE160 4.6 0.5 1.0 CA A:THR162 4.6 0.7 1.0 N A:ASN163 4.7 0.4 1.0 CB A:ILE160 4.7 0.6 1.0 HB A:ILE160 4.7 1.0 1.0 CA A:ASN163 4.7 0.2 1.0 HB A:THR162 4.8 0.8 1.0 HB3 A:ASN163 4.9 0.7 1.0 CA A:GLY156 4.9 0.4 1.0 CD A:GLN19 4.9 0.6 1.0 NE2 A:GLN19 4.9 0.3 1.0 HA A:ASP157 4.9 0.6 1.0 H A:ILE160 4.9 0.8 1.0 H A:TYR161 4.9 0.2 1.0

Magnesium binding site 2 out of 3 in the Hslu L199Q in Hsluv Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hslu L199Q in Hsluv Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg201 b:48.3 occ:1.00 O B:THR162 2.9 0.6 1.0 O B:GLY156 3.0 0.5 1.0 HA B:ILE160 3.4 0.7 1.0 O B:CYS159 3.4 0.6 1.0 HA B:ASN163 3.9 1.0 1.0 O B:ILE160 3.9 0.6 1.0 C B:THR162 4.1 0.7 1.0 C B:GLY156 4.2 0.6 1.0 CA B:ILE160 4.2 0.1 1.0 C B:ILE160 4.3 99.2 1.0 HE1 B:HIS164 4.3 0.5 1.0 OE1 B:GLN19 4.4 0.2 1.0 C B:CYS159 4.4 1.0 1.0 H B:THR162 4.5 0.3 1.0 HG21 D:VAL26 4.5 0.8 1.0 HA B:ASP157 4.6 0.7 1.0 HA2 B:GLY156 4.6 0.7 1.0 CA B:ASN163 4.7 1.0 1.0 N B:ILE160 4.8 0.6 1.0 HE22 B:GLN19 4.8 0.7 1.0 N B:ASN163 4.9 0.7 1.0 HB3 B:ASN163 4.9 0.4 1.0 CE1 B:HIS164 4.9 0.4 1.0 N B:THR162 4.9 0.1 1.0 CA B:GLY156 4.9 0.8 1.0

Magnesium binding site 3 out of 3 in the Hslu L199Q in Hsluv Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Hslu L199Q in Hsluv Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg201 b:60.5 occ:1.00 O D:THR162 2.1 98.4 1.0 O D:GLY156 2.2 97.7 1.0 O D:CYS159 3.0 0.2 1.0 HA D:ASN163 3.2 0.1 1.0 C D:GLY156 3.3 98.7 1.0 C D:THR162 3.4 100.0 1.0 HA2 D:GLY156 3.6 0.8 1.0 HA D:ILE160 3.7 0.4 1.0 CA D:GLY156 4.0 99.0 1.0 H D:THR162 4.0 0.4 1.0 HE1 D:HIS164 4.0 0.7 1.0 CA D:ASN163 4.1 0.5 1.0 HA3 D:GLY156 4.1 0.8 1.0 N D:ASN163 4.1 0.2 1.0 HA D:ASP157 4.2 0.8 1.0 C D:CYS159 4.2 0.8 1.0 O D:ILE160 4.2 0.9 1.0 OE1 D:GLN19 4.3 1.0 1.0 N D:ASP157 4.4 0.9 1.0 N D:THR162 4.4 0.8 1.0 CA D:ILE160 4.4 99.5 1.0 CA D:THR162 4.4 0.0 1.0 C D:ILE160 4.4 0.5 1.0 HB D:THR162 4.5 0.4 1.0 CE1 D:HIS164 4.5 0.8 1.0 HB3 D:ASN163 4.6 0.3 1.0 CA D:ASP157 4.7 0.9 1.0 HG21 B:VAL26 4.8 0.3 1.0 N D:ILE160 4.8 96.4 1.0 ND1 D:HIS164 4.8 0.7 1.0 CB D:ASN163 4.8 0.3 1.0 C D:ASP157 4.9 0.7 1.0 H D:ASN163 5.0 0.5 1.0

V.Baytshtok, X.Fei, R.A.Grant, T.A.Baker, R.T.Sauer. A Structurally Dynamic Region of the Hslu Intermediate Domain Controls Protein Degradation and Atp Hydrolysis. Structure V. 24 1766 2016.
ISSN: ISSN 1878-4186
PubMed: 27667691
DOI: 10.1016/J.STR.2016.08.012