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Chlorine in PDB 4uyz: Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A

Enzymatic activity of Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A

All present enzymatic activity of Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A:
3.1.1.1;

Protein crystallography data

The structure of Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A, PDB code: 4uyz 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) 96.94 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.829, 193.880, 75.717, 90.00, 91.88, 90.00
R / Rfree (%) 24.761 / 29.294

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A (pdb code 4uyz). 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 II - 2.8A, PDB code: 4uyz:

Chlorine binding site 1 out of 1 in 4uyz

Go back to Chlorine Binding Sites List in 4uyz
Chlorine binding site 1 out of 1 in the Structure of the Wnt Deacylase Notum - Crystal Form II - 2.8A


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 II - 2.8A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1453

b:72.2
occ:1.00
NE B:ARG416 3.5 99.5 1.0
CE1 B:HIS412 3.7 46.0 1.0
NH2 B:ARG409 3.8 52.9 1.0
CZ B:ARG416 3.9 0.7 1.0
NH2 B:ARG416 4.0 0.6 1.0
CD B:ARG416 4.2 91.4 1.0
NH1 B:ARG409 4.2 51.6 1.0
ND1 B:HIS412 4.4 45.3 1.0
CZ B:ARG409 4.5 52.0 1.0
NE2 B:HIS412 4.8 45.2 1.0
NH1 B:ARG416 4.9 0.2 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: Fri Jul 26 02:36:57 2024

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