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Chlorine in PDB 4uz9: Structure of the Wnt Deacylase Notum - Crystal Form VII - Sos Complex - 2.2A

Enzymatic activity of Structure of the Wnt Deacylase Notum - Crystal Form VII - Sos Complex - 2.2A

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

Protein crystallography data

The structure of Structure of the Wnt Deacylase Notum - Crystal Form VII - Sos Complex - 2.2A, PDB code: 4uz9 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) 65.58 / 2.20
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 69.630, 69.630, 195.148, 90.00, 90.00, 90.00
R / Rfree (%) 19.007 / 23.653

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Wnt Deacylase Notum - Crystal Form VII - Sos Complex - 2.2A (pdb code 4uz9). 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 VII - Sos Complex - 2.2A, PDB code: 4uz9:

Chlorine binding site 1 out of 1 in 4uz9

Go back to Chlorine Binding Sites List in 4uz9
Chlorine binding site 1 out of 1 in the Structure of the Wnt Deacylase Notum - Crystal Form VII - Sos Complex - 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 VII - Sos Complex - 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1454

b:64.8
occ:1.00
NH2 A:ARG90 3.4 60.2 1.0
CE1 A:HIS92 3.8 33.2 1.0
NH1 A:ARG218 3.8 44.0 1.0
NH2 A:ARG218 3.8 45.5 1.0
ND1 A:HIS92 4.2 33.0 1.0
CZ A:ARG218 4.3 43.3 1.0
CZ A:ARG90 4.6 63.7 1.0
NH1 A:ARG90 4.9 67.7 1.0
NE2 A:HIS92 5.0 31.7 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 02:37:14 2024

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