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Zinc in PDB 1i4g: Crystal Structure of Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity, PDB code: 1i4g was solved by M.Hakansson, P.Antonsson, P.Bjork, L.A.Svensson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.660, 84.830, 86.350, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity (pdb code 1i4g). 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 Crystal Structure of Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity, PDB code: 1i4g:

Zinc binding site 1 out of 1 in 1i4g

Go back to Zinc Binding Sites List in 1i4g
Zinc binding site 1 out of 1 in the Crystal Structure of Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity


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 Staphylococcal Enterotoxin A Mutant H187A with Reduced ZN2+ Affinity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn460

b:23.2
occ:0.60
O A:HOH507 1.8 24.9 1.0
OD2 A:ASP227 2.0 27.4 1.0
NE2 A:HIS225 2.2 30.2 1.0
CG A:ASP227 2.8 27.9 1.0
OD1 A:ASP227 2.9 28.6 1.0
CD2 A:HIS225 3.0 26.2 1.0
CE1 A:HIS225 3.3 30.6 1.0
O A:HOH580 3.7 55.4 1.0
CB A:ASP227 4.2 25.5 1.0
CB A:ALA187 4.2 25.4 1.0
CG A:HIS225 4.3 28.6 1.0
ND1 A:HIS225 4.4 34.5 1.0
ND2 A:ASN128 4.6 17.4 1.0

Reference:

M.Hakansson, P.Antonsson, P.Bjork, L.A.Svensson. Cooperative Zinc Binding in A Staphylococcal Enterotoxin A Mutant Mimics the Sea-Mhc Class II Interaction J.Biol.Inorg.Chem. V. 6 757 2001.
ISSN: ISSN 0949-8257
PubMed: 11713682
DOI: 10.1007/S007750100251
Page generated: Wed Dec 16 02:52:15 2020

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