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Sodium in PDB 8qnh: Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23)

Protein crystallography data

The structure of Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23), PDB code: 8qnh was solved by M.Schimpl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.80 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.04, 73.594, 93.973, 90, 90, 90
R / Rfree (%) 22.2 / 24.8

Other elements in 8qnh:

The structure of Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23) also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23) (pdb code 8qnh). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23), PDB code: 8qnh:

Sodium binding site 1 out of 1 in 8qnh

Go back to Sodium Binding Sites List in 8qnh
Sodium binding site 1 out of 1 in the Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the E3 Ubiquitin Ligase Cbl-B with An Allosteric Inhibitor (WO2020264398 EX23) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na504

b:27.2
occ:1.00
OD1 A:ASP221 2.3 29.4 1.0
O A:TYR227 2.3 31.2 1.0
OD1 A:ASN225 2.3 28.9 1.0
OE2 A:GLU232 2.3 38.2 1.0
OG1 A:THR223 2.6 32.1 1.0
OE1 A:GLU232 2.6 35.5 1.0
CD A:GLU232 2.8 38.0 1.0
O A:HOH612 2.8 35.6 1.0
CG A:ASN225 3.3 29.4 1.0
CG A:ASP221 3.4 31.4 1.0
C A:TYR227 3.4 30.5 1.0
ND2 A:ASN225 3.9 28.8 1.0
CB A:THR223 3.9 31.1 1.0
CA A:ASP221 4.0 28.9 1.0
N A:THR223 4.0 29.2 1.0
N A:TYR227 4.1 30.7 1.0
CB A:ASP221 4.1 28.7 1.0
N A:ASN225 4.1 30.9 1.0
OD2 A:ASP221 4.3 33.1 1.0
CA A:TYR227 4.3 30.4 1.0
C A:ASP221 4.3 29.9 1.0
CA A:THR223 4.3 29.9 1.0
CG A:GLU232 4.3 33.4 1.0
N A:ILE228 4.4 29.5 1.0
N A:CYS224 4.4 30.9 1.0
CG2 A:THR223 4.4 31.0 1.0
CA A:ILE228 4.4 29.2 1.0
C A:THR223 4.4 30.9 1.0
N A:LEU222 4.5 29.2 1.0
CB A:ASN225 4.5 30.2 1.0
CB A:TYR227 4.5 31.3 1.0
CA A:ASN225 4.7 31.1 1.0
N A:ASP226 4.8 33.6 1.0
N A:SER229 4.9 28.7 1.0
CD1 A:ILE228 4.9 30.4 1.0
O A:ASP221 4.9 30.2 1.0
C A:ASN225 4.9 32.9 1.0

Reference:

M.Schimpl, M.Schimpl. N/A N/A.
Page generated: Wed Oct 9 13:11:52 2024

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