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Chlorine in PDB 5jqs: Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin

Protein crystallography data

The structure of Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin, PDB code: 5jqs was solved by S.A.Abdul Rehman, Y.Kulathu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.63 / 2.65
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.336, 82.336, 332.464, 90.00, 90.00, 120.00
R / Rfree (%) 20.5 / 23.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin (pdb code 5jqs). 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 Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin, PDB code: 5jqs:

Chlorine binding site 1 out of 1 in 5jqs

Go back to Chlorine Binding Sites List in 5jqs
Chlorine binding site 1 out of 1 in the Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Deubiquitinase Mindy-1 in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:62.1
occ:1.00
NE2 A:GLN149 3.1 42.4 1.0
N A:LEU311 3.5 42.2 1.0
O A:HOH519 3.6 46.5 1.0
O A:GLY309 3.6 35.9 1.0
CA A:GLU310 3.9 40.9 1.0
CB A:LEU311 4.1 34.3 1.0
CG A:LEU311 4.2 34.4 1.0
C A:GLU310 4.2 40.9 1.0
CD A:GLN149 4.3 36.8 1.0
O A:HOH545 4.4 76.7 1.0
CA A:LEU311 4.4 32.4 1.0
CD1 A:LEU311 4.4 39.6 1.0
CG A:GLU310 4.5 46.5 1.0
CG A:GLN149 4.6 39.5 1.0
C A:GLY309 4.6 31.8 1.0
CB A:GLU310 4.7 36.7 1.0
N A:GLU310 4.7 41.6 1.0
O A:LEU311 4.8 30.6 1.0

Reference:

S.A.Abdul Rehman, Y.A.Kristariyanto, S.Y.Choi, P.J.Nkosi, S.Weidlich, K.Labib, K.Hofmann, Y.Kulathu. Mindy-1 Is A Member of An Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. Mol.Cell V. 63 146 2016.
ISSN: ISSN 1097-2765
PubMed: 27292798
DOI: 10.1016/J.MOLCEL.2016.05.009
Page generated: Sat Dec 12 11:54:03 2020

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