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Zinc in PDB 1ck1: Structure of Staphylococcal Enterotoxin C3

Protein crystallography data

The structure of Structure of Staphylococcal Enterotoxin C3, PDB code: 1ck1 was solved by Y.-I.Chi, G.A.Bohach, C.V.Stauffacher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.60
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 43.700, 43.700, 280.500, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 23.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Staphylococcal Enterotoxin C3 (pdb code 1ck1). 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 Structure of Staphylococcal Enterotoxin C3, PDB code: 1ck1:

Zinc binding site 1 out of 1 in 1ck1

Go back to Zinc Binding Sites List in 1ck1
Zinc binding site 1 out of 1 in the Structure of Staphylococcal Enterotoxin C3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Staphylococcal Enterotoxin C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:33.2
occ:1.00
OD2 A:ASP83 2.2 32.3 1.0
ND1 A:HIS118 2.2 22.4 1.0
NE2 A:HIS122 2.2 19.8 1.0
CG A:ASP83 2.9 32.2 1.0
OD1 A:ASP83 3.0 32.0 1.0
CE1 A:HIS118 3.0 26.0 1.0
CD2 A:HIS122 3.2 23.9 1.0
CE1 A:HIS122 3.2 26.4 1.0
CG A:HIS118 3.4 32.2 1.0
CB A:HIS118 3.8 37.1 1.0
CA A:HIS118 4.0 32.9 1.0
O A:HIS118 4.1 39.8 1.0
NE2 A:HIS118 4.2 36.0 1.0
O A:HOH330 4.2 20.3 1.0
ND1 A:HIS122 4.3 25.8 1.0
CG A:HIS122 4.3 25.8 1.0
CB A:ASP83 4.4 27.0 1.0
CD2 A:HIS118 4.4 35.6 1.0
C A:HIS118 4.5 36.7 1.0
CG A:LYS37 4.6 26.0 1.0

Reference:

Y.I.Chi, I.Sadler, L.M.Jablonski, S.D.Callantine, C.F.Deobald, C.V.Stauffacher, G.A.Bohach. Zinc-Mediated Dimerization and Its Effect on Activity and Conformation of Staphylococcal Enterotoxin Type C. J.Biol.Chem. V. 277 22839 2002.
ISSN: ISSN 0021-9258
PubMed: 11934896
DOI: 10.1074/JBC.M201932200
Page generated: Wed Dec 16 02:46:32 2020

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