Manganese in PDB 5f1m: Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus

All present enzymatic activity of Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus:
3.1.3.16;

The structure of Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus, PDB code: 5f1m was solved by W.H.Zheng, T.Wang, Z.G.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.11 / 2.32
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.770, 77.350, 85.360, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 25.6

The binding sites of Manganese atom in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus (pdb code 5f1m). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus, PDB code: 5f1m:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus


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 Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:21.0 occ:0.62 OD2 A:ASP233 1.7 43.3 1.0 OD1 A:ASP194 2.2 28.3 1.0 OD1 A:ASP37 2.2 33.3 1.0 O A:HOH479 2.2 22.2 1.0 O A:HOH430 2.2 26.4 1.0 O A:HOH453 2.3 18.0 1.0 CG A:ASP233 2.8 43.0 1.0 CG A:ASP37 3.1 34.3 1.0 OD2 A:ASP37 3.2 37.9 1.0 CG A:ASP194 3.2 27.8 1.0 OD1 A:ASP233 3.3 42.4 1.0 OD2 A:ASP194 3.5 27.7 1.0 MN A:MN302 3.6 17.2 0.3 O A:HOH455 3.6 27.2 1.0 CB A:ASP233 4.1 43.7 1.0 N A:GLY195 4.1 29.9 1.0 O A:HOH437 4.2 35.2 1.0 O A:HOH460 4.3 42.0 1.0 O A:HOH457 4.3 32.3 1.0 O A:HOH443 4.4 22.8 1.0 CB A:ASP37 4.5 31.4 1.0 CB A:ASP194 4.6 27.2 1.0 OD1 A:ASP19 4.6 34.9 1.0 O A:ASN234 4.6 35.1 1.0 N A:ASP194 4.6 26.9 1.0 CA A:GLY195 4.7 29.8 1.0 C A:ASP194 4.7 29.6 1.0 O A:HOH407 4.9 20.5 1.0 CA A:ASP194 4.9 28.0 1.0 CB A:SER193 4.9 24.1 1.0 OG A:SER193 5.0 24.0 1.0 O A:HOH414 5.0 39.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus


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 Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:17.2 occ:0.33 O A:HOH453 1.8 18.0 1.0 O A:HOH407 1.8 20.5 1.0 OD2 A:ASP37 1.9 37.9 1.0 O A:GLY38 2.0 28.5 1.0 O A:HOH437 2.0 35.2 1.0 O A:HOH455 2.3 27.2 1.0 CG A:ASP37 3.1 34.3 1.0 C A:GLY38 3.2 29.0 1.0 MN A:MN301 3.6 21.0 0.6 N A:GLY38 3.7 29.2 1.0 OD1 A:ASP37 3.7 33.3 1.0 OD1 A:ASP19 3.9 34.9 1.0 C A:ASP37 4.0 30.6 1.0 CA A:GLY38 4.0 28.2 1.0 N A:GLY40 4.0 33.8 1.0 O A:HOH479 4.0 22.2 1.0 O A:HOH471 4.0 20.4 1.0 O A:HOH430 4.1 26.4 1.0 N A:MET39 4.2 30.0 1.0 CB A:GLU18 4.2 33.7 1.0 NH1 A:ARG14 4.3 93.9 1.0 OD1 A:ASP233 4.3 42.4 1.0 CB A:ASP37 4.3 31.4 1.0 CA A:MET39 4.3 31.2 1.0 CA A:ASP37 4.4 29.8 1.0 C A:MET39 4.4 32.7 1.0 O A:ASP37 4.4 31.3 1.0 OE2 A:GLU18 4.4 37.5 1.0 OD2 A:ASP233 4.6 43.3 1.0 OD1 A:ASN234 4.6 42.4 1.0 O A:GLU18 4.6 34.4 1.0 C A:GLU18 4.7 33.7 1.0 CA A:GLY40 4.8 35.8 1.0 CG A:ASP233 4.9 43.0 1.0 CG A:GLU18 5.0 35.6 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus


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 Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn303 b:68.5 occ:0.89 O A:HOH472 2.1 74.8 1.0 O A:HOH510 2.2 69.6 1.0 O A:HOH410 2.3 44.1 1.0 O A:HOH498 2.5 50.9 1.0 OE1 A:GLU18 2.5 37.5 1.0 O A:HOH456 2.8 40.2 1.0 CD A:GLU18 3.6 36.7 1.0 O A:HIS42 3.8 41.5 1.0 OE2 A:GLU18 3.9 37.5 1.0 N A:ALA44 4.2 42.0 1.0 O A:GLY40 4.3 38.9 1.0 NZ A:LYS16 4.4 72.6 1.0 CD A:LYS16 4.4 74.0 1.0 N A:GLY45 4.5 36.0 1.0 OE2 A:GLU46 4.5 36.9 1.0 C A:LYS43 4.8 41.6 1.0 O A:HOH532 4.8 49.8 1.0 CA A:ALA44 4.9 39.2 1.0 CG A:GLU18 4.9 35.6 1.0 CA A:LYS43 4.9 42.1 1.0 CA A:GLY40 5.0 35.8 1.0 CE A:LYS16 5.0 72.8 1.0 C A:HIS42 5.0 41.4 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Serine/Threonine Phosphatase STP1 From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn304 b:38.9 occ:0.40 O A:HOH414 1.9 39.6 1.0 O A:HOH451 2.0 37.6 1.0 OD2 A:ASP120 2.0 36.2 1.0 O A:HOH422 2.0 45.0 1.0 O A:HOH423 2.1 48.5 1.0 OD2 A:ASP194 2.3 27.7 1.0 CG A:ASP120 3.3 34.7 1.0 CG A:ASP194 3.3 27.8 1.0 CB A:ASP194 3.6 27.2 1.0 OD2 A:ASP198 3.8 29.6 1.0 O A:ARG161 3.8 38.8 1.0 CD1 A:ILE164 4.0 49.2 1.0 O A:HOH457 4.0 32.3 1.0 OD1 A:ASP120 4.1 35.2 1.0 CA A:ASN162 4.2 40.0 1.0 CB A:ASP120 4.3 30.4 1.0 O A:ASN162 4.4 39.9 1.0 O A:HOH479 4.4 22.2 1.0 OD1 A:ASP194 4.4 28.3 1.0 O A:HOH467 4.4 34.8 1.0 C A:ASN162 4.5 40.5 1.0 OD1 A:ASP198 4.5 32.9 1.0 O A:HOH425 4.6 23.6 1.0 CG A:ASP198 4.6 31.5 1.0 C A:ARG161 4.8 39.7 1.0 N A:ASN162 5.0 39.6 1.0

W.Zheng, X.Cai, M.Xie, Y.Liang, T.Wang, Z.Li. Structure-Based Identification of A Potent Inhibitor Targeting STP1-Mediated Virulence Regulation in Staphylococcus Aureus Cell Chem Biol V. 23 1002 2016.
ISSN: ESSN 2451-9456
PubMed: 27499528
DOI: 10.1016/J.CHEMBIOL.2016.06.014