Magnesium in PDB 6ihs: Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation

All present enzymatic activity of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation:
3.1.3.16;

The structure of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation, PDB code: 6ihs was solved by C.-G.Yang, T.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.793, 86.355, 38.896, 90.00, 90.00, 90.00
R / Rfree (%)	13 / 16.8

The binding sites of Magnesium atom in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation (pdb code 6ihs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation, PDB code: 6ihs:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:16.2 occ:1.00 OD2 A:ASP118 2.0 16.7 1.0 O A:HOH417 2.0 17.8 1.0 OD2 A:ASP192 2.1 16.1 1.0 O A:HOH455 2.1 15.9 1.0 O A:HOH487 2.1 14.9 1.0 O A:HOH421 2.1 17.2 1.0 CG A:ASP118 3.2 14.5 1.0 CG A:ASP192 3.2 14.1 1.0 CB A:ASP192 3.6 13.8 1.0 O A:HOH472 3.8 17.4 1.0 OD2 A:ASP196 3.9 18.3 1.0 OD1 A:ASP118 3.9 14.6 1.0 O A:HOH431 4.1 15.3 1.0 O A:ARG159 4.1 17.6 1.0 O A:HOH481 4.2 28.1 1.0 CB A:ASP118 4.2 14.4 1.0 O A:ASN160 4.2 16.3 1.0 CA A:ASN160 4.3 16.3 1.0 O A:HOH441 4.3 15.4 1.0 OD1 A:ASP192 4.3 13.9 1.0 OD1 A:ASP196 4.3 18.0 1.0 OD1 A:ASN160 4.5 22.2 1.0 CG A:ASP196 4.5 16.4 1.0 C A:ASN160 4.6 15.9 1.0 CG2 A:ILE162 4.7 23.1 1.0 O A:HOH531 4.8 24.7 1.0 C A:ARG159 5.0 16.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:14.6 occ:1.00 OD1 A:ASP192 2.0 13.9 1.0 O A:HOH431 2.1 15.3 1.0 OD2 A:ASP231 2.1 15.4 1.0 OD2 A:ASP35 2.1 13.5 1.0 O A:HOH484 2.1 14.8 1.0 O A:HOH404 2.2 14.8 1.0 CG A:ASP35 3.0 12.1 1.0 CG A:ASP192 3.1 14.1 1.0 CG A:ASP231 3.1 14.9 1.0 OD1 A:ASP231 3.4 15.3 1.0 OD1 A:ASP35 3.4 13.0 1.0 OD2 A:ASP192 3.5 16.1 1.0 MG A:MG303 3.8 14.3 1.0 N A:GLY193 4.1 14.5 1.0 O A:HOH478 4.2 13.8 1.0 O A:HOH463 4.2 21.6 1.0 O A:HOH531 4.2 24.7 1.0 OD1 A:ASP17 4.3 14.9 1.0 CB A:ASP35 4.3 13.2 1.0 O A:HOH435 4.3 14.1 1.0 O A:HOH472 4.4 17.4 1.0 CB A:ASP231 4.4 16.3 1.0 CB A:ASP192 4.4 13.8 1.0 N A:ASP192 4.4 13.3 1.0 O A:ASN232 4.5 15.1 1.0 C A:ASP192 4.6 14.4 1.0 CA A:ASP192 4.7 13.8 1.0 CB A:SER191 4.8 13.8 1.0 CA A:GLY193 4.9 15.4 1.0 OG A:SER191 4.9 14.8 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:14.3 occ:1.00 OD1 A:ASP35 2.0 13.0 1.0 O A:GLY36 2.1 15.1 1.0 O A:HOH476 2.1 15.1 1.0 O A:HOH435 2.1 14.1 1.0 O A:HOH404 2.2 14.8 1.0 CG A:ASP35 3.1 12.1 1.0 C A:GLY36 3.2 14.8 1.0 OD2 A:ASP35 3.7 13.5 1.0 MG A:MG302 3.8 14.6 1.0 N A:GLY36 3.8 13.9 1.0 O A:HOH498 3.9 15.1 1.0 N A:GLY38 3.9 17.7 1.0 C A:ASP35 4.0 13.3 1.0 CA A:GLY36 4.1 13.1 1.0 OD1 A:ASP17 4.1 14.9 1.0 O A:HOH431 4.1 15.3 1.0 N A:MET37 4.2 14.5 1.0 CA A:MET37 4.3 15.7 1.0 CB A:GLU16 4.3 15.5 1.0 O A:HOH484 4.3 14.8 1.0 CB A:ASP35 4.3 13.2 1.0 O A:HOH488 4.3 20.4 1.0 OE1 A:GLU16 4.4 17.3 1.0 OD1 A:ASP231 4.4 15.3 1.0 C A:MET37 4.4 17.9 1.0 O A:ASP35 4.4 13.9 1.0 ND2 A:ASN232 4.5 12.4 1.0 CA A:ASP35 4.5 12.9 1.0 NH1 A:ARG12 4.5 21.0 1.0 CA A:GLY38 4.7 17.5 1.0 O A:GLU16 4.8 14.1 1.0 C A:GLU16 4.9 13.4 1.0 OD2 A:ASP231 5.0 15.4 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Bacterial Serine Phosphatase with His-Tag Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:19.6 occ:1.00 O A:HOH552 2.0 22.6 1.0 OE2 A:GLU16 2.0 18.5 1.0 O A:HOH440 2.1 21.0 1.0 O A:HOH521 2.1 21.3 1.0 O A:HOH427 2.1 19.4 1.0 O A:HOH447 2.1 17.3 1.0 CD A:GLU16 3.1 17.2 1.0 OE1 A:GLU16 3.5 17.3 1.0 O A:HOH523 4.0 26.0 1.0 O A:GLY38 4.2 18.6 1.0 OE1 A:GLU44 4.3 21.6 1.0 O A:HIS40 4.3 19.2 1.0 CG A:GLU16 4.3 15.2 1.0 O A:HOH541 4.3 29.5 1.0 N A:GLY43 4.4 16.1 1.0 N A:ALA42 4.5 17.4 1.0 CA A:GLY38 4.7 17.5 1.0 C A:GLY38 4.9 18.6 1.0 O A:MET37 5.0 19.1 1.0

T.Yang, T.Liu, J.Gan, K.Yu, K.Chen, W.Xue, L.Lan, S.Yang, C.G.Yang. Structural Insight Into the Mechanism of Staphylococcus Aureus STP1 Phosphatase. Acs Infect Dis. V. 5 841 2019.
ISSN: ESSN 2373-8227
PubMed: 30868877
DOI: 10.1021/ACSINFECDIS.8B00316