Chlorine in PDB 5xyz: The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor

Enzymatic activity of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor

All present enzymatic activity of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor:
2.7.10.2;

Protein crystallography data

The structure of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor, PDB code: 5xyz was solved by Y.L.Wang, Y.Z.Sun, R.Cao, D.Liu, Y.T.Xie, L.Li, X.B.Qi, N.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.16 / 2.64
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.590, 53.600, 101.635, 90.00, 100.04, 90.00
R / Rfree (%) 26.5 / 32.6

Other elements in 5xyz:

The structure of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor (pdb code 5xyz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor, PDB code: 5xyz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5xyz

Go back to Chlorine Binding Sites List in 5xyz
Chlorine binding site 1 out of 2 in the The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl701

b:82.0
occ:1.00
CL7 A:GYL701 0.0 82.0 1.0
C1 A:GYL701 1.7 72.0 1.0
C6 A:GYL701 2.6 69.0 1.0
C2 A:GYL701 2.7 67.5 1.0
C8 A:GYL701 3.0 68.3 1.0
N15 A:GYL701 3.1 69.9 1.0
CG2 A:VAL416 3.3 73.7 1.0
CB A:LYS430 3.7 77.3 1.0
OG1 A:THR474 3.9 57.2 1.0
N A:LYS430 3.9 62.8 1.0
C5 A:GYL701 3.9 67.5 1.0
C A:ILE429 4.0 58.6 1.0
C17 A:GYL701 4.0 70.9 1.0
C3 A:GYL701 4.0 64.3 1.0
CG2 A:THR474 4.0 55.2 1.0
O A:ALA428 4.1 46.9 1.0
N A:ILE429 4.2 46.8 1.0
C A:ALA428 4.2 45.7 1.0
O A:ILE472 4.2 53.6 1.0
CA A:ILE429 4.3 53.9 1.0
CB A:ALA428 4.3 46.6 1.0
CA A:LYS430 4.4 69.8 1.0
O A:ILE429 4.4 56.5 1.0
C4 A:GYL701 4.5 64.4 1.0
CB A:THR474 4.6 55.7 1.0
N18 A:GYL701 4.7 69.9 1.0
CB A:VAL416 4.7 76.7 1.0
N21 A:GYL701 4.7 64.0 1.0
CD A:LYS430 4.7 92.8 1.0
CG A:LYS430 4.8 80.5 1.0
N A:THR474 4.8 57.6 1.0
CA A:ALA428 4.9 45.3 1.0
C A:ILE472 5.0 60.6 1.0

Chlorine binding site 2 out of 2 in 5xyz

Go back to Chlorine Binding Sites List in 5xyz
Chlorine binding site 2 out of 2 in the The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structure of Human Btk Kinase Domain in Complex with A Covalent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl701

b:70.6
occ:1.00
CL7 B:GYL701 0.0 70.6 1.0
C1 B:GYL701 1.8 69.8 1.0
C2 B:GYL701 2.7 66.0 1.0
C6 B:GYL701 2.8 65.0 1.0
C8 B:GYL701 3.0 60.3 1.0
N15 B:GYL701 3.0 61.3 1.0
OG1 B:THR474 3.4 67.6 1.0
CG2 B:VAL416 3.5 66.6 1.0
CB B:LYS430 3.5 67.6 1.0
N B:LYS430 3.6 64.2 1.0
C17 B:GYL701 3.9 59.0 1.0
CB B:ALA428 3.9 59.1 1.0
C B:ILE429 4.0 61.8 1.0
O B:ILE472 4.0 68.1 1.0
CA B:LYS430 4.0 64.7 1.0
C3 B:GYL701 4.0 63.1 1.0
C5 B:GYL701 4.1 61.1 1.0
N B:ILE429 4.1 60.8 1.0
C B:ALA428 4.1 61.2 1.0
CG2 B:THR474 4.2 60.6 1.0
O B:ALA428 4.2 58.6 1.0
CD B:LYS430 4.3 80.8 1.0
CB B:THR474 4.4 62.9 1.0
CA B:ILE429 4.4 62.0 1.0
CG B:LYS430 4.4 73.9 1.0
O B:ILE429 4.5 53.1 1.0
N18 B:GYL701 4.5 55.8 1.0
C4 B:GYL701 4.6 58.8 1.0
N21 B:GYL701 4.6 53.1 1.0
CA B:ALA428 4.6 60.2 1.0
CB B:VAL416 4.7 62.4 1.0
N B:THR474 4.9 63.0 1.0

Reference:

Y.Wang, Y.Sun, R.Cao, D.Liu, Y.Xie, L.Li, X.Qi, N.Huang. In Silico Identification of A Novel Hinge-Binding Scaffold For Kinase Inhibitor Discovery. J. Med. Chem. V. 60 8552 2017.
ISSN: ISSN 1520-4804
PubMed: 28945083
DOI: 10.1021/ACS.JMEDCHEM.7B01075
Page generated: Sat Dec 12 12:39:52 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy