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Chlorine in PDB 3usq: Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270

Enzymatic activity of Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270

All present enzymatic activity of Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270:
2.4.1.186;

Protein crystallography data

The structure of Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270, PDB code: 3usq was solved by F.M.Issoglio, M.E.Carrizo, J.M.Romero, J.A.Curtino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.32 / 2.40
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 56.530, 105.640, 120.080, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270 (pdb code 3usq). 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 Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270, PDB code: 3usq:

Chlorine binding site 1 out of 1 in 3usq

Go back to Chlorine Binding Sites List in 3usq
Chlorine binding site 1 out of 1 in the Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of D159S/Y194F Glycogenin Mutant Truncated at Residue 270 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl273

b:2.0
occ:0.25
O A:HOH275 3.0 20.2 1.0
N A:ILE178 3.3 17.2 1.0
CG2 A:ILE178 3.5 16.4 1.0
CA A:ASP177 3.8 17.5 1.0
CB A:ILE178 4.0 17.5 1.0
C A:ASP177 4.0 17.5 1.0
CA A:ILE178 4.2 18.0 1.0
OD1 A:ASP177 4.3 15.5 1.0
N A:ASP177 4.4 17.6 1.0
N A:ARG179 4.9 19.9 1.0
CB A:ASP177 4.9 16.9 1.0

Reference:

F.M.Issoglio, M.E.Carrizo, J.M.Romero, J.A.Curtino. Mechanisms of Monomeric and Dimeric Glycogenin Autoglucosylation. J.Biol.Chem. V. 287 1955 2012.
ISSN: ISSN 0021-9258
PubMed: 22128147
DOI: 10.1074/JBC.M111.287813
Page generated: Sat Dec 12 10:15:58 2020

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