Zinc in PDB 1eu4: Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes

The structure of Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes, PDB code: 1eu4 was solved by V.L.Arcus, T.Proft, J.A.Sigrell, H.M.Baker, J.D.Fraser, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.49 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	36.629, 46.028, 64.470, 90.00, 91.64, 90.00
R / Rfree (%)	20.5 / 25.8

The binding sites of Zinc atom in the Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes (pdb code 1eu4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes, PDB code: 1eu4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:35.0 occ:1.00 NE2 A:HIS198 2.1 25.6 1.0 OD1 A:ASP160 2.1 30.0 1.0 OD1 A:ASP200 2.1 27.9 1.0 O A:HOH431 2.6 39.0 1.0 CE1 A:HIS198 2.8 26.2 1.0 CG A:ASP200 2.9 23.3 1.0 OD2 A:ASP200 3.0 21.7 1.0 CG A:ASP160 3.1 30.4 1.0 CD2 A:HIS198 3.3 25.2 1.0 CB A:ASP160 3.4 28.4 1.0 ND1 A:HIS198 4.0 25.7 1.0 OD2 A:ASP160 4.2 34.8 1.0 CG A:HIS198 4.3 26.1 1.0 CB A:ASP200 4.3 21.0 1.0 ND2 A:ASN105 4.8 26.3 1.0 CA A:ASP160 4.9 26.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Superantigen Spe-H (Zinc Bound) From Streptococcus Pyogenes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:61.6 occ:1.00 OD2 A:ASP160 2.0 34.8 1.0 O A:HOH416 2.6 35.9 1.0 CG A:ASP160 3.0 30.4 1.0 OD1 A:ASP160 3.4 30.0 1.0 O A:LEU161 3.8 29.8 1.0 OD1 A:ASP166 3.9 40.8 1.0 OD2 A:ASP166 4.1 38.3 1.0 CB A:ASP160 4.4 28.4 1.0 CG A:ASP166 4.4 37.4 1.0 CA A:ASP160 4.6 26.1 1.0 C A:ASP160 4.6 26.8 1.0 N A:LEU161 4.7 28.4 1.0 C A:LEU161 4.8 29.8 1.0

V.L.Arcus, T.Proft, J.A.Sigrell, H.M.Baker, J.D.Fraser, E.N.Baker. Conservation and Variation in Superantigen Structure and Activity Highlighted By the Three-Dimensional Structures of Two New Superantigens From Streptococcus Pyogenes. J.Mol.Biol. V. 299 157 2000.
ISSN: ISSN 0022-2836
PubMed: 10860729
DOI: 10.1006/JMBI.2000.3725