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Chlorine in PDB 4uz7: Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A

Enzymatic activity of Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A

All present enzymatic activity of Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A:
3.1.1.1;

Protein crystallography data

The structure of Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A, PDB code: 4uz7 was solved by M.Zebisch, E.Y.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.80 / 2.20
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.863, 79.925, 160.004, 90.00, 94.04, 90.00
R / Rfree (%) 18.271 / 22.864

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A (pdb code 4uz7). 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 Wnt Deacylase Notum - Crystal Form VI - 2.2A, PDB code: 4uz7:

Chlorine binding site 1 out of 1 in 4uz7

Go back to Chlorine Binding Sites List in 4uz7
Chlorine binding site 1 out of 1 in the Structure of the Wnt Deacylase Notum - Crystal Form VI - 2.2A


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 Wnt Deacylase Notum - Crystal Form VI - 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1452

b:59.7
occ:1.00
N A:SER395 3.1 25.6 1.0
OG A:SER395 3.5 33.8 1.0
CB A:SER395 3.6 32.3 1.0
CA A:ARG394 3.7 24.0 1.0
C A:ARG394 3.9 24.4 1.0
CA A:SER395 3.9 29.9 1.0
CB A:ARG394 4.2 26.9 1.0
O A:ILE393 4.4 20.7 1.0
CD2 A:HIS396 4.7 34.3 1.0
CG A:ARG394 4.8 30.1 1.0
N A:ARG394 4.9 21.0 1.0
CB A:THR159 4.9 20.0 1.0

Reference:

S.Kakugawa, P.F.Langton, M.Zebisch, S.A.Howell, T.-H.Chang, Y.Liu, T.Feizi, G.Bineva, N.O'reilly, A.P.Snijders, E.Y.Jones, J.-P.Vincent. Notum Deacylates Wnt Proteins to Suppress Signalling Activity Nature 2015.
ISSN: ESSN 1476-4687
DOI: 10.1038/NATURE14259
Page generated: Sat Dec 12 11:16:42 2020

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