Chlorine in PDB 6qhk: Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S

Enzymatic activity of Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S

All present enzymatic activity of Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S:
2.3.2.23;

Protein crystallography data

The structure of Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S, PDB code: 6qhk was solved by A.K.L.Liess, S.Lorenz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.42 / 1.96
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 83.150, 83.150, 83.125, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 22.3

Other elements in 6qhk:

The structure of Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S also contains other interesting chemical elements:

Arsenic (As) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S (pdb code 6qhk). 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 Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S, PDB code: 6qhk:

Chlorine binding site 1 out of 1 in 6qhk

Go back to Chlorine Binding Sites List in 6qhk
Chlorine binding site 1 out of 1 in the Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pao-Linked Dimer of the Catalytic Domain of the Human Ubiquitin- Conjugating Enzyme UBE2S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:26.2
occ:1.00
 H A:ASN91 2.4 30.5 1.0
H A:GLU93 2.5 24.8 1.0
HB2 A:ASN91 2.7 41.5 1.0
HA3 A:GLY89 2.8 33.0 1.0
HB3 A:GLU93 2.9 33.4 1.0
N A:ASN91 3.2 25.4 1.0
O A:HOH336 3.3 41.9 1.0
HB2 A:GLU93 3.3 33.4 1.0
N A:GLU93 3.3 20.6 1.0
H A:GLY92 3.4 32.6 1.0
CB A:GLU93 3.5 27.9 1.0
CB A:ASN91 3.5 34.5 1.0
CA A:ASN91 3.6 27.7 1.0
N A:GLY92 3.6 27.2 1.0
C A:ASN91 3.6 28.0 1.0
CA A:GLY89 3.6 27.5 1.0
C A:GLY89 3.7 28.5 1.0
H A:ALA90 3.7 29.8 1.0
N A:ALA90 3.8 24.8 1.0
HD22 A:ASN91 3.9 40.4 1.0
CA A:GLU93 4.0 20.2 1.0
H A:GLY89 4.1 27.9 1.0
HB3 A:ASN91 4.1 41.5 1.0
O A:ASN91 4.3 29.2 1.0
HA2 A:GLY89 4.3 33.0 1.0
O A:GLY89 4.3 23.2 1.0
C A:ALA90 4.3 30.8 1.0
C A:GLY92 4.4 22.2 1.0
N A:GLY89 4.4 23.3 1.0
CG A:ASN91 4.4 32.0 1.0
ND2 A:ASN91 4.4 33.7 1.0
CA A:GLY92 4.5 27.9 1.0
HA A:ASN91 4.5 33.3 1.0
CA A:ALA90 4.6 28.8 1.0
OE2 A:GLU93 4.7 40.2 1.0
HA A:GLU93 4.7 24.3 1.0
O A:GLU93 4.8 22.5 1.0
HD2 A:TYR78 4.8 51.4 1.0
CG A:GLU93 4.9 33.5 1.0
HB3 A:ALA90 4.9 48.0 1.0
C A:GLU93 4.9 21.1 1.0

Reference:

A.K.L.Liess, A.Kucerova, K.Schweimer, L.Yu, T.I.Roumeliotis, M.Diebold, O.Dybkov, C.Sotriffer, H.Urlaub, J.S.Choudhary, J.Mansfeld, S.Lorenz. Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S By Autoubiquitination. Structure V. 27 1195 2019.
ISSN: ISSN 0969-2126
PubMed: 31230944
DOI: 10.1016/J.STR.2019.05.008
Page generated: Sat Dec 12 13:33:41 2020

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