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Fluorine in PDB 6yg6: Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105

Enzymatic activity of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105

All present enzymatic activity of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105:
2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105, PDB code: 6yg6 was solved by A.Chaikuad, L.Tan, J.Wang, Y.Liang, N.S.Gray, S.Knapp, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.33 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.651, 69.934, 73.763, 90.00, 119.36, 90.00
R / Rfree (%) 20.4 / 23.9

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 (pdb code 6yg6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105, PDB code: 6yg6:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 6yg6

Go back to Fluorine Binding Sites List in 6yg6
Fluorine binding site 1 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:47.4
occ:1.00
 F2 A:OQ8502 0.0 47.4 1.0
C7 A:OQ8502 1.3 44.3 1.0
F A:OQ8502 2.1 41.7 1.0
F1 A:OQ8502 2.1 45.1 1.0
C6 A:OQ8502 2.4 40.4 1.0
C5 A:OQ8502 3.1 46.1 1.0
C4 A:OQ8502 3.2 49.2 1.0
CD2 A:HIS257 3.2 38.7 1.0
C11 A:OQ8502 3.4 39.3 1.0
NE2 A:HIS257 3.5 39.7 1.0
C A:CYS276 3.9 38.2 1.0
O A:CYS276 3.9 34.2 1.0
C2 A:OQ8502 3.9 50.5 1.0
CD1 A:LEU249 4.1 38.4 1.0
N1 A:OQ8502 4.1 49.8 1.0
N A:ASP277 4.2 40.4 1.0
CG A:LEU275 4.2 33.8 1.0
CA A:CYS276 4.2 35.8 1.0
CD2 A:LEU275 4.3 34.7 1.0
C8 A:OQ8502 4.4 44.6 1.0
CB A:ASP277 4.4 43.8 1.0
CG A:HIS257 4.5 38.5 1.0
N A:CYS276 4.6 34.5 1.0
C10 A:OQ8502 4.6 38.9 1.0
O A:LEU275 4.7 32.8 1.0
C A:LEU275 4.8 34.2 1.0
CE1 A:HIS257 4.8 40.2 1.0
CA A:ASP277 4.9 41.6 1.0
C3 A:OQ8502 4.9 52.8 1.0

Fluorine binding site 2 out of 6 in 6yg6

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Fluorine binding site 2 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:45.1
occ:1.00
 F1 A:OQ8502 0.0 45.1 1.0
C7 A:OQ8502 1.3 44.3 1.0
F A:OQ8502 2.1 41.7 1.0
F2 A:OQ8502 2.1 47.4 1.0
C6 A:OQ8502 2.4 40.4 1.0
C4 A:OQ8502 3.0 49.2 1.0
C5 A:OQ8502 3.0 46.1 1.0
C11 A:OQ8502 3.5 39.3 1.0
CG2 A:VAL186 3.6 46.9 0.5
CG2 A:ILE195 3.9 39.2 1.0
CD1 A:LEU249 4.0 38.4 1.0
CD2 A:LEU249 4.0 40.2 1.0
CG2 A:VAL186 4.1 43.6 0.5
CB A:VAL186 4.2 44.5 0.5
C8 A:OQ8502 4.3 44.6 1.0
N1 A:OQ8502 4.3 49.8 1.0
CB A:VAL186 4.5 47.2 0.5
CG A:LEU249 4.6 38.8 1.0
CA A:VAL186 4.6 46.3 0.5
C10 A:OQ8502 4.6 38.9 1.0
CA A:VAL186 4.7 47.7 0.5
CG1 A:ILE195 4.7 38.3 1.0
CG1 A:VAL186 4.8 46.9 0.5
CD1 A:ILE195 4.8 40.4 1.0
C2 A:OQ8502 4.8 50.5 1.0
C3 A:OQ8502 5.0 52.8 1.0
C9 A:OQ8502 5.0 41.6 1.0
CB A:ILE195 5.0 39.1 1.0

Fluorine binding site 3 out of 6 in 6yg6

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Fluorine binding site 3 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:41.7
occ:1.00
 F A:OQ8502 0.0 41.7 1.0
C7 A:OQ8502 1.3 44.3 1.0
F2 A:OQ8502 2.1 47.4 1.0
F1 A:OQ8502 2.1 45.1 1.0
C6 A:OQ8502 2.4 40.4 1.0
C11 A:OQ8502 2.7 39.3 1.0
O A:LEU275 3.5 32.8 1.0
CA A:CYS276 3.5 35.8 1.0
CG2 A:ILE195 3.6 39.2 1.0
C5 A:OQ8502 3.7 46.1 1.0
C A:CYS276 3.8 38.2 1.0
C A:LEU275 3.9 34.2 1.0
N A:CYS276 4.0 34.5 1.0
C10 A:OQ8502 4.1 38.9 1.0
N A:ASP277 4.1 40.4 1.0
CG1 A:VAL196 4.1 41.6 1.0
CG2 A:VAL186 4.1 43.6 0.5
O2 A:OQ8502 4.2 40.4 1.0
C4 A:OQ8502 4.3 49.2 1.0
CG2 A:VAL186 4.3 46.9 0.5
O A:CYS276 4.4 34.2 1.0
CB A:CYS276 4.6 36.9 1.0
CB A:ILE195 4.7 39.1 1.0
C8 A:OQ8502 4.8 44.6 1.0
CB A:VAL186 4.8 44.5 0.5
N A:VAL196 4.8 37.5 1.0
CG A:LEU275 4.8 33.8 1.0
CG1 A:ILE195 4.8 38.3 1.0
CG1 A:VAL186 4.8 46.9 0.5
C9 A:OQ8502 4.9 41.6 1.0
N2 A:OQ8502 5.0 39.1 1.0
C12 A:OQ8502 5.0 40.8 1.0
CB A:LEU275 5.0 33.6 1.0

Fluorine binding site 4 out of 6 in 6yg6

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Fluorine binding site 4 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F504

b:52.8
occ:1.00
 F2 B:OQ8504 0.0 52.8 1.0
C7 B:OQ8504 1.3 53.0 1.0
F1 B:OQ8504 2.1 53.0 1.0
F B:OQ8504 2.1 53.4 1.0
C6 B:OQ8504 2.3 49.6 1.0
C5 B:OQ8504 3.1 50.6 1.0
CD2 B:HIS257 3.1 53.2 1.0
C4 B:OQ8504 3.2 51.2 1.0
NE2 B:HIS257 3.3 54.3 1.0
C11 B:OQ8504 3.3 49.5 1.0
O B:CYS276 3.7 49.7 1.0
C B:CYS276 3.7 51.4 1.0
CG B:LEU275 4.0 44.7 1.0
N B:ASP277 4.0 54.0 1.0
CA B:CYS276 4.1 49.6 1.0
CD2 B:LEU275 4.1 45.8 1.0
C2 B:OQ8504 4.1 58.5 1.0
CD1 B:LEU249 4.2 53.0 1.0
N1 B:OQ8504 4.2 56.3 1.0
C8 B:OQ8504 4.3 48.5 1.0
CB B:ASP277 4.4 60.4 1.0
N B:CYS276 4.4 47.5 1.0
CG B:HIS257 4.4 52.4 1.0
C10 B:OQ8504 4.5 49.7 1.0
C B:LEU275 4.5 47.2 1.0
O B:LEU275 4.5 49.0 1.0
CE1 B:HIS257 4.6 52.9 1.0
CA B:ASP277 4.8 56.8 1.0
CB B:LEU275 4.8 44.8 1.0
CD1 B:LEU275 4.9 43.9 1.0
C9 B:OQ8504 4.9 48.6 1.0

Fluorine binding site 5 out of 6 in 6yg6

Go back to Fluorine Binding Sites List in 6yg6
Fluorine binding site 5 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F504

b:53.0
occ:1.00
 F1 B:OQ8504 0.0 53.0 1.0
C7 B:OQ8504 1.3 53.0 1.0
F2 B:OQ8504 2.1 52.8 1.0
F B:OQ8504 2.1 53.4 1.0
C6 B:OQ8504 2.4 49.6 1.0
C4 B:OQ8504 3.0 51.2 1.0
C5 B:OQ8504 3.0 50.6 1.0
C11 B:OQ8504 3.5 49.5 1.0
CD1 B:LEU249 3.8 53.0 1.0
CG2 B:ILE195 3.8 54.8 1.0
CG2 B:VAL186 3.9 67.3 0.5
CD2 B:LEU249 4.1 55.1 1.0
C8 B:OQ8504 4.3 48.5 1.0
N1 B:OQ8504 4.4 56.3 1.0
CG B:LEU249 4.5 53.1 1.0
CG1 B:ILE195 4.6 54.8 1.0
CB B:VAL186 4.6 68.1 0.5
C10 B:OQ8504 4.7 49.7 1.0
CD1 B:ILE195 4.8 58.0 1.0
CB B:ILE195 4.9 53.7 1.0
CG2 B:VAL186 4.9 66.5 0.5
CD2 B:HIS257 4.9 53.2 1.0
C2 B:OQ8504 4.9 58.5 1.0
CB B:VAL186 4.9 68.0 0.5
O B:LEU275 5.0 49.0 1.0
C9 B:OQ8504 5.0 48.6 1.0

Fluorine binding site 6 out of 6 in 6yg6

Go back to Fluorine Binding Sites List in 6yg6
Fluorine binding site 6 out of 6 in the Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of MKK7 (MAP2K7) Covalently Bound with Type-II Inhibitor TL10-105 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F504

b:53.4
occ:1.00
 F B:OQ8504 0.0 53.4 1.0
C7 B:OQ8504 1.3 53.0 1.0
F2 B:OQ8504 2.1 52.8 1.0
F1 B:OQ8504 2.1 53.0 1.0
C6 B:OQ8504 2.4 49.6 1.0
C11 B:OQ8504 2.7 49.5 1.0
O B:LEU275 3.2 49.0 1.0
CA B:CYS276 3.3 49.6 1.0
C5 B:OQ8504 3.7 50.6 1.0
C B:LEU275 3.7 47.2 1.0
C B:CYS276 3.7 51.4 1.0
CG2 B:ILE195 3.8 54.8 1.0
N B:CYS276 3.8 47.5 1.0
CG1 B:VAL196 4.0 48.5 1.0
N B:ASP277 4.0 54.0 1.0
C10 B:OQ8504 4.1 49.7 1.0
O2 B:OQ8504 4.2 54.2 1.0
O B:CYS276 4.3 49.7 1.0
C4 B:OQ8504 4.4 51.2 1.0
CB B:CYS276 4.5 49.8 1.0
CG2 B:VAL186 4.5 67.3 0.5
CG B:LEU275 4.6 44.7 1.0
N B:VAL196 4.6 48.5 1.0
CB B:ILE195 4.7 53.7 1.0
CB B:LEU275 4.8 44.8 1.0
C8 B:OQ8504 4.8 48.5 1.0
CG1 B:ILE195 4.8 54.8 1.0
CA B:LEU275 4.9 44.7 1.0
CG2 B:VAL186 4.9 66.5 0.5
C9 B:OQ8504 4.9 48.6 1.0
N2 B:OQ8504 5.0 49.0 1.0
C12 B:OQ8504 5.0 49.4 1.0
CD2 B:LEU275 5.0 45.8 1.0
O B:VAL196 5.0 49.8 1.0
CA B:ILE195 5.0 50.5 1.0

Reference:

M.Schroder, L.Tan, J.Wang, Y.Liang, N.S.Gray, S.Knapp, A.Chaikuad. Catalytic Domain Plasticity of MKK7 Reveals Structural Mechanisms of Allosteric Activation and Diverse Targeting Opportunities. Cell Chem Biol V. 27 1285 2020.
ISSN: ESSN 2451-9456
PubMed: 32783966
DOI: 10.1016/J.CHEMBIOL.2020.07.014
Page generated: Fri Aug 2 04:30:22 2024

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