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Zinc in PDB 1ste: Staphylococcal Enterotoxin C2 From Staphylococcus Aureus

Protein crystallography data

The structure of Staphylococcal Enterotoxin C2 From Staphylococcus Aureus, PDB code: 1ste was solved by K.R.Acharya, A.C.Papageorgiou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 43.050, 43.050, 290.000, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Staphylococcal Enterotoxin C2 From Staphylococcus Aureus (pdb code 1ste). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Staphylococcal Enterotoxin C2 From Staphylococcus Aureus, PDB code: 1ste:

Zinc binding site 1 out of 1 in 1ste

Go back to Zinc Binding Sites List in 1ste
Zinc binding site 1 out of 1 in the Staphylococcal Enterotoxin C2 From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Staphylococcal Enterotoxin C2 From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:11.7
occ:1.00
OD2 A:ASP83 1.9 9.5 1.0
NE2 A:HIS122 2.2 10.5 1.0
ND1 A:HIS118 2.2 13.9 1.0
CG A:ASP83 2.7 9.7 1.0
OD1 A:ASP83 2.9 7.8 1.0
CE1 A:HIS118 3.0 10.7 1.0
CD2 A:HIS122 3.0 13.7 1.0
CE1 A:HIS122 3.2 13.7 1.0
CG A:HIS118 3.3 11.4 1.0
CB A:HIS118 3.7 10.6 1.0
CA A:HIS118 3.9 10.9 1.0
O A:HOH351 4.1 32.7 1.0
O A:HOH327 4.1 11.4 1.0
NE2 A:HIS118 4.1 14.1 1.0
CB A:ASP83 4.2 8.1 1.0
O A:HIS118 4.2 13.4 1.0
CG A:HIS122 4.2 12.2 1.0
ND1 A:HIS122 4.3 15.5 1.0
CD2 A:HIS118 4.3 11.7 1.0
C A:HIS118 4.4 14.3 1.0
CG2 A:THR36 4.5 20.4 1.0
CG A:LYS37 4.9 23.6 1.0

Reference:

A.C.Papageorgiou, K.R.Acharya, R.Shapiro, E.F.Passalacqua, R.D.Brehm, H.S.Tranter. Crystal Structure of the Superantigen Enterotoxin C2 From Staphylococcus Aureus Reveals A Zinc-Binding Site. Structure V. 3 769 1995.
ISSN: ISSN 0969-2126
PubMed: 7582894
DOI: 10.1016/S0969-2126(01)00212-X
Page generated: Mon Jan 25 16:13:29 2021

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