Potassium in PDB 2rdg: Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X

The structure of Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X, PDB code: 2rdg was solved by M.C.Chung, B.D.Wines, H.Baker, R.J.Langley, E.N.Baker, J.D.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.45 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.031, 57.945, 43.462, 90.00, 101.83, 90.00
R / Rfree (%)	17.4 / 20.7

The binding sites of Potassium atom in the Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X (pdb code 2rdg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X, PDB code: 2rdg:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X within 5.0Å range: probe atom residue distance (Å) B Occ A:K605 b:19.1 occ:0.75 O A:ASN100 2.6 23.5 1.0 O A:HOH944 2.7 42.5 1.0 O A:HOH664 2.7 21.7 1.0 OE1 A:GLN99 2.9 26.8 1.0 O A:HOH832 2.9 30.4 1.0 O A:HOH859 3.0 29.0 1.0 CD A:GLN99 3.6 26.7 1.0 C A:ASN100 3.8 23.5 1.0 NE2 A:GLN99 4.2 28.6 1.0 O A:HOH916 4.2 65.8 1.0 O A:HOH945 4.4 41.2 1.0 N A:ASN100 4.5 22.9 1.0 NZ A:LYS162 4.6 30.5 1.0 CG1 A:VAL101 4.6 23.8 1.0 O A:HOH910 4.6 36.6 1.0 CG A:GLN99 4.6 23.7 1.0 CA A:VAL101 4.6 22.8 1.0 N A:VAL101 4.7 22.9 1.0 CA A:ASN100 4.7 23.4 1.0

Potassium binding site 2 out of 3 in the Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X within 5.0Å range: probe atom residue distance (Å) B Occ A:K606 b:15.7 occ:0.75 O2 A:CIT608 2.8 21.6 1.0 OE1 A:GLN11 2.8 21.1 1.0 O7 A:CIT608 2.9 21.5 1.0 O A:HOH854 3.0 20.5 1.0 O6 A:CIT608 3.0 24.4 1.0 OE1 A:GLN8 3.2 24.7 1.0 O A:HOH902 3.3 38.6 1.0 O A:HOH757 3.6 27.8 1.0 C6 A:CIT608 3.7 23.9 1.0 C3 A:CIT608 3.8 23.8 1.0 C1 A:CIT608 3.8 23.9 1.0 CD A:GLN11 3.9 21.6 1.0 CD A:GLN8 4.0 23.1 1.0 NE2 A:GLN8 4.0 22.6 1.0 NE2 A:GLN11 4.3 21.5 1.0 C2 A:CIT608 4.4 22.5 1.0 O3 A:CIT608 4.7 24.2 1.0 O5 A:CIT608 4.8 24.5 1.0 O1 A:CIT608 4.8 23.3 1.0

Potassium binding site 3 out of 3 in the Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X within 5.0Å range: probe atom residue distance (Å) B Occ A:K607 b:29.1 occ:0.75 O A:GLY110 2.9 31.0 1.0 O A:HOH752 2.9 27.9 1.0 OG A:SER108 3.0 27.6 1.0 O A:THR113 3.1 22.7 1.0 O A:GLN111 3.6 30.5 1.0 OG1 A:THR114 3.8 25.1 1.0 CB A:SER108 3.8 27.4 1.0 N A:THR113 3.9 24.4 1.0 C A:THR113 3.9 23.4 1.0 C A:GLN111 4.0 30.0 1.0 C A:GLY110 4.1 31.0 1.0 CA A:SER108 4.2 27.3 1.0 C A:HIS112 4.4 25.7 1.0 N A:HIS112 4.4 28.5 1.0 CA A:THR113 4.5 23.7 1.0 CA A:HIS112 4.6 26.9 1.0 N A:THR114 4.7 22.4 1.0 CA A:GLN111 4.7 30.7 1.0 N A:GLY110 4.9 30.8 1.0 N A:THR109 4.9 29.3 1.0 N A:GLN111 4.9 30.8 1.0 C A:SER108 5.0 28.3 1.0

M.C.Chung, B.D.Wines, H.Baker, R.J.Langley, E.N.Baker, J.D.Fraser. The Crystal Structure of Staphylococcal Superantigen-Like Protein 11 in Complex with Sialyl Lewis X Reveals the Mechanism For Cell Binding and Immune Inhibition Mol.Microbiol. V. 66 1342 2007.
ISSN: ISSN 0950-382X
PubMed: 18045383
DOI: 10.1111/J.1365-2958.2007.05989.X