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Chlorine in PDB 2cbi: Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase

Enzymatic activity of Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase

All present enzymatic activity of Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase:
3.2.1.35;

Protein crystallography data

The structure of Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase, PDB code: 2cbi was solved by F.V.Rao, H.C.Dorfmueller, F.Villa, M.Allwood, I.M.Eggleston, D.M.F.Vanaalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.25
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 119.939, 147.380, 157.687, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 22

Other elements in 2cbi:

The structure of Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase also contains other interesting chemical elements:

Zinc (Zn) 11 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase (pdb code 2cbi). 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 the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase, PDB code: 2cbi:

Chlorine binding site 1 out of 1 in 2cbi

Go back to Chlorine Binding Sites List in 2cbi
Chlorine binding site 1 out of 1 in the Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Clostridium Perfringens Nagj Family 84 Glycoside Hydrolase, A Homologue of Human O-Glcnacase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1626

b:32.0
occ:1.00
 O A:HOH2063 2.6 32.2 1.0
OD1 A:ASN208 2.8 10.4 1.0
NE2 A:HIS442 3.1 7.4 1.0
CE A:MET466 3.4 6.5 1.0
NE2 A:GLN161 3.4 10.2 1.0
CD2 A:HIS442 3.4 3.9 1.0
CG A:ASN208 3.7 9.8 1.0
ND2 A:ASN208 3.9 7.5 1.0
SD A:MET466 4.1 9.0 1.0
CB A:ASN47 4.3 9.6 1.0
CE1 A:HIS442 4.4 4.2 1.0
CB A:MET466 4.5 8.6 1.0
ND2 A:ASN47 4.5 7.6 1.0
CD A:GLN161 4.5 13.9 1.0
O A:ASN47 4.7 10.3 1.0
CG A:HIS442 4.7 8.0 1.0
CG A:MET466 4.8 9.0 1.0
CG A:ASN47 4.9 9.6 1.0

Reference:

F.V.Rao, H.C.Dorfmueller, F.Villa, M.Allwood, I.M.Eggleston, D.M.Van Aalten. Structural Insights Into the Mechanism and Inhibition of Eukaryotic O-Glcnac Hydrolysis. Embo J. V. 25 1569 2006.
ISSN: ISSN 0261-4189
PubMed: 16541109
DOI: 10.1038/SJ.EMBOJ.7601026
Page generated: Thu Jul 10 21:42:43 2025

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