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Chlorine in PDB 4gof: Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38

Protein crystallography data

The structure of Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38, PDB code: 4gof was solved by J.W.Chartron, D.G.Vandervelde, W.M.Clemons Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.39 / 1.35
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 29.607, 43.608, 63.468, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 19.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38 (pdb code 4gof). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38, PDB code: 4gof:

Chlorine binding site 1 out of 1 in 4gof

Go back to Chlorine Binding Sites List in 4gof
Chlorine binding site 1 out of 1 in the Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Sgta Homodimerization Domain with Covalent Modifications to Both C38 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl102

b:14.5
occ:0.50
NH1 A:ARG20 3.2 14.0 1.0
CE1 A:HIS16 3.6 14.1 1.0
CD A:ARG20 3.8 12.3 1.0
CG A:ARG20 4.2 11.2 1.0
CZ A:ARG20 4.2 13.6 1.0
NE2 A:HIS16 4.4 14.8 1.0
NE A:ARG20 4.4 12.4 1.0
ND1 A:HIS16 4.6 12.9 1.0
OE2 A:GLU48 4.9 13.7 1.0
O A:HOH228 5.0 25.1 1.0

Reference:

J.W.Chartron, D.G.Vandervelde, W.M.Clemons. Structures of the SGT2/Sgta Dimerization Domain with the GET5/UBL4A Ubl Domain Reveal An Interaction That Forms A Conserved Dynamic Interface. Cell Rep V. 2 1620 2012.
ISSN: ESSN 2211-1247
PubMed: 23142665
DOI: 10.1016/J.CELREP.2012.10.010
Page generated: Sat Dec 12 10:40:15 2020

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