Chlorine in PDB 6heh: Structure of the Catalytic Domain of USP28 (Insertion Deleted)

Enzymatic activity of Structure of the Catalytic Domain of USP28 (Insertion Deleted)

All present enzymatic activity of Structure of the Catalytic Domain of USP28 (Insertion Deleted):
3.4.19.12;

Protein crystallography data

The structure of Structure of the Catalytic Domain of USP28 (Insertion Deleted), PDB code: 6heh was solved by M.Gersch, D.Komander, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.55 / 2.26
Space group I 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 189.152, 189.152, 189.152, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 21.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Catalytic Domain of USP28 (Insertion Deleted) (pdb code 6heh). 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 Catalytic Domain of USP28 (Insertion Deleted), PDB code: 6heh:

Chlorine binding site 1 out of 1 in 6heh

Go back to Chlorine Binding Sites List in 6heh
Chlorine binding site 1 out of 1 in the Structure of the Catalytic Domain of USP28 (Insertion Deleted)


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 Catalytic Domain of USP28 (Insertion Deleted) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl802

b:37.1
occ:1.00
O A:HOH922 3.2 42.8 1.0
NE2 A:GLN390 3.3 28.7 1.0
O A:HOH980 3.5 39.8 1.0
OE1 A:GLN390 3.9 30.5 1.0
CD A:GLN390 4.1 30.3 1.0
CB A:TRP626 4.2 28.7 1.0
CE1 A:TYR606 4.3 35.8 1.0
NE1 A:TRP613 4.3 32.6 1.0
CD1 A:TRP613 4.4 28.8 1.0
O A:HOH952 4.8 38.3 1.0
OH A:TYR606 4.8 39.4 1.0
CG A:TRP626 4.8 34.5 1.0

Reference:

M.Gersch, J.L.Wagstaff, A.V.Toms, B.Graves, S.M.V.Freund, D.Komander. Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity. Mol.Cell V. 74 436 2019.
ISSN: ISSN 1097-2765
PubMed: 30926242
DOI: 10.1016/J.MOLCEL.2019.02.030
Page generated: Sat Dec 12 13:04:51 2020

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