Chlorine in PDB 6fnm: Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib
Enzymatic activity of Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib
All present enzymatic activity of Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib:
2.7.10.1;
Protein crystallography data
The structure of Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib, PDB code: 6fnm
was solved by
D.Kudlinzki,
A.Troester,
K.Witt,
V.L.Linhard,
K.Saxena,
H.Schwalbe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.04 /
1.16
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.941,
54.111,
62.162,
90.00,
110.45,
90.00
|
R / Rfree (%)
|
18.4 /
19.5
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib
(pdb code 6fnm). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the
Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib, PDB code: 6fnm:
Jump to Chlorine binding site number:
1;
2;
Chlorine binding site 1 out
of 2 in 6fnm
Go back to
Chlorine Binding Sites List in 6fnm
Chlorine binding site 1 out
of 2 in the Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib
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 Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1001
b:18.8
occ:0.44
|
CL
|
A:1N11001
|
0.0
|
18.8
|
0.4
|
C10
|
A:1N11001
|
0.2
|
20.1
|
0.4
|
C9
|
A:1N11001
|
1.6
|
17.9
|
0.4
|
C5
|
A:1N11001
|
1.7
|
17.8
|
0.4
|
C8
|
A:1N11001
|
2.5
|
17.8
|
0.4
|
C4
|
A:1N11001
|
2.7
|
15.8
|
0.4
|
C6
|
A:1N11001
|
2.7
|
17.6
|
0.4
|
C4
|
A:1N11001
|
2.8
|
15.9
|
0.4
|
N2
|
A:1N11001
|
3.0
|
15.8
|
0.4
|
N2
|
A:1N11001
|
3.0
|
15.8
|
0.4
|
O
|
A:ALA645
|
3.2
|
16.4
|
1.0
|
C
|
A:ALA645
|
3.4
|
16.1
|
1.0
|
O
|
A:ILE691
|
3.4
|
17.8
|
1.0
|
OG1
|
A:THR693
|
3.5
|
17.6
|
1.0
|
N
|
A:LYS647
|
3.6
|
17.8
|
1.0
|
N
|
A:ILE646
|
3.6
|
16.5
|
1.0
|
C3
|
A:1N11001
|
3.7
|
16.2
|
0.4
|
C3
|
A:1N11001
|
3.7
|
16.3
|
0.4
|
CB
|
A:ALA645
|
3.7
|
16.4
|
1.0
|
CA
|
A:ILE646
|
3.8
|
17.6
|
1.0
|
C7
|
A:1N11001
|
3.8
|
19.7
|
0.4
|
CG2
|
A:THR693
|
3.8
|
17.0
|
1.0
|
C
|
A:ILE646
|
3.8
|
18.9
|
1.0
|
N
|
A:THR693
|
3.9
|
16.1
|
1.0
|
C5
|
A:1N11001
|
3.9
|
16.2
|
0.4
|
CG
|
A:LYS647
|
3.9
|
21.6
|
1.0
|
C7
|
A:1N11001
|
4.0
|
19.7
|
0.4
|
C9
|
A:1N11001
|
4.1
|
16.5
|
0.4
|
O
|
A:1N11001
|
4.1
|
18.4
|
0.4
|
O
|
A:1N11001
|
4.1
|
18.5
|
0.4
|
CB
|
A:THR693
|
4.2
|
17.4
|
1.0
|
CA
|
A:ALA645
|
4.2
|
16.6
|
1.0
|
C
|
A:ILE691
|
4.2
|
16.7
|
1.0
|
CB
|
A:LYS647
|
4.3
|
18.9
|
1.0
|
C6
|
A:1N11001
|
4.4
|
19.3
|
0.4
|
C
|
A:LEU692
|
4.4
|
16.4
|
1.0
|
CA
|
A:LEU692
|
4.4
|
16.3
|
1.0
|
C8
|
A:1N11001
|
4.5
|
19.5
|
0.4
|
CA
|
A:LYS647
|
4.5
|
19.6
|
1.0
|
C2
|
A:1N11001
|
4.6
|
15.7
|
0.4
|
C2
|
A:1N11001
|
4.6
|
15.7
|
0.4
|
O
|
A:ILE646
|
4.6
|
20.0
|
1.0
|
CA
|
A:THR693
|
4.6
|
15.8
|
1.0
|
N
|
A:LEU692
|
4.7
|
17.5
|
1.0
|
CD
|
A:LYS647
|
4.8
|
23.1
|
1.0
|
CG2
|
A:ILE691
|
4.9
|
18.8
|
1.0
|
CE
|
A:LYS647
|
4.9
|
22.8
|
1.0
|
|
Chlorine binding site 2 out
of 2 in 6fnm
Go back to
Chlorine Binding Sites List in 6fnm
Chlorine binding site 2 out
of 2 in the Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Crystal Structure of Ephrin B4 (EPHB4) Receptor Protein Kinase with Dasatinib within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1001
b:18.2
occ:0.44
|
CL
|
A:1N11001
|
0.0
|
18.2
|
0.4
|
C10
|
A:1N11001
|
0.2
|
18.3
|
0.4
|
C9
|
A:1N11001
|
1.5
|
16.5
|
0.4
|
C5
|
A:1N11001
|
1.7
|
16.2
|
0.4
|
C8
|
A:1N11001
|
2.5
|
19.5
|
0.4
|
C4
|
A:1N11001
|
2.6
|
15.9
|
0.4
|
C6
|
A:1N11001
|
2.7
|
19.3
|
0.4
|
C4
|
A:1N11001
|
2.7
|
15.8
|
0.4
|
N2
|
A:1N11001
|
3.0
|
15.8
|
0.4
|
N2
|
A:1N11001
|
3.0
|
15.8
|
0.4
|
C3
|
A:1N11001
|
3.4
|
16.2
|
0.4
|
C3
|
A:1N11001
|
3.4
|
16.3
|
0.4
|
O
|
A:1N11001
|
3.4
|
18.5
|
0.4
|
O
|
A:1N11001
|
3.5
|
18.4
|
0.4
|
O
|
A:HOH1121
|
3.5
|
30.4
|
1.0
|
CB
|
A:SER757
|
3.7
|
21.6
|
1.0
|
O
|
A:HOH1120
|
3.8
|
32.4
|
1.0
|
C7
|
A:1N11001
|
3.8
|
19.7
|
0.4
|
C5
|
A:1N11001
|
3.9
|
17.8
|
0.4
|
O
|
A:HOH1218
|
3.9
|
32.1
|
1.0
|
C7
|
A:1N11001
|
4.0
|
19.7
|
0.4
|
CD1
|
A:LEU747
|
4.0
|
18.1
|
1.0
|
C9
|
A:1N11001
|
4.0
|
17.9
|
0.4
|
CG2
|
A:ILE677
|
4.1
|
16.6
|
0.5
|
CG2
|
A:ILE677
|
4.1
|
16.3
|
0.5
|
CG1
|
A:ILE677
|
4.2
|
14.7
|
0.5
|
O
|
A:HOH1131
|
4.2
|
34.5
|
1.0
|
CE
|
A:MET668
|
4.3
|
10.9
|
0.5
|
C6
|
A:1N11001
|
4.3
|
17.6
|
0.4
|
OG
|
A:SER757
|
4.4
|
24.5
|
1.0
|
C2
|
A:1N11001
|
4.4
|
15.7
|
0.4
|
C2
|
A:1N11001
|
4.4
|
15.7
|
0.4
|
CG1
|
A:ILE677
|
4.5
|
15.1
|
0.5
|
C8
|
A:1N11001
|
4.5
|
17.8
|
0.4
|
OE2
|
A:GLU664
|
4.6
|
24.4
|
1.0
|
CB
|
A:ILE677
|
4.6
|
14.6
|
0.5
|
CB
|
A:ILE677
|
4.6
|
15.0
|
0.5
|
SD
|
A:MET668
|
4.7
|
32.7
|
0.5
|
N
|
A:ASP758
|
4.8
|
19.3
|
1.0
|
CA
|
A:SER757
|
4.8
|
17.5
|
1.0
|
CG2
|
A:THR693
|
4.9
|
17.0
|
1.0
|
CD1
|
A:ILE677
|
4.9
|
17.0
|
0.5
|
CE
|
A:LYS647
|
4.9
|
22.8
|
1.0
|
C1
|
A:1N11001
|
5.0
|
16.6
|
0.4
|
NZ
|
A:LYS647
|
5.0
|
25.4
|
1.0
|
C1
|
A:1N11001
|
5.0
|
16.5
|
0.4
|
|
Reference:
A.Troster,
S.Heinzlmeir,
B.T.Berger,
S.L.Gande,
K.Saxena,
S.Sreeramulu,
V.Linhard,
A.H.Nasiri,
M.Bolte,
S.Muller,
B.Kuster,
G.Medard,
D.Kudlinzki,
H.Schwalbe.
Nvp-BHG712: Effects of Regioisomers on the Affinity and Selectivity Toward the Ephrin Family. Chemmedchem V. 13 1629 2018.
ISSN: ESSN 1860-7187
PubMed: 29928781
DOI: 10.1002/CMDC.201800398
Page generated: Sat Dec 12 12:59:16 2020
|