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Chlorine in PDB 5oq3: High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile

Enzymatic activity of High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile

All present enzymatic activity of High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile:
3.5.1.28;

Protein crystallography data

The structure of High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile, PDB code: 5oq3 was solved by W.J.Bradshaw, J.M.Kirby, A.K.Roberts, C.C.Shone, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.51 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.016, 65.639, 104.010, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 17.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile (pdb code 5oq3). 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 High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile, PDB code: 5oq3:

Chlorine binding site 1 out of 1 in 5oq3

Go back to Chlorine Binding Sites List in 5oq3
Chlorine binding site 1 out of 1 in the High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Structure of the Functional Region of CWP19 From Clostridium Difficile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:15.5
occ:1.00
NH1 A:ARG232 3.2 9.2 1.0
NH2 A:ARG232 3.3 10.6 1.0
CZ A:ARG232 3.7 8.6 1.0
O A:HOH893 3.9 24.5 1.0

Reference:

W.J.Bradshaw, J.M.Kirby, A.K.Roberts, C.C.Shone, K.R.Acharya. The Molecular Structure of the Glycoside Hydrolase Domain of CWP19 From Clostridium Difficile. Febs J. V. 284 4343 2017.
ISSN: ISSN 1742-4658
PubMed: 29083543
DOI: 10.1111/FEBS.14310
Page generated: Sat Dec 12 12:13:18 2020

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