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Fluorine in PDB 4g3f: Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2)

Enzymatic activity of Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2)

All present enzymatic activity of Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2):
2.7.11.25;

Protein crystallography data

The structure of Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2), PDB code: 4g3f was solved by S.G.Hymowitz, G.De Leon-Boenig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.23 / 1.64
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 74.789, 135.619, 64.857, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.8

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2) (pdb code 4g3f). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2), PDB code: 4g3f:

Fluorine binding site 1 out of 1 in 4g3f

Go back to Fluorine Binding Sites List in 4g3f
Fluorine binding site 1 out of 1 in the Crystal Structure of Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2)


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 Murine Nf-Kappab Inducing Kinase (Nik) Bound to A 2-(Aminothiazoly)Phenol (CMP2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F701

b:15.6
occ:1.00
 F6 A:0WB701 0.0 15.6 1.0
C5 A:0WB701 1.4 13.0 1.0
C7 A:0WB701 2.4 13.4 1.0
C4 A:0WB701 2.4 11.1 1.0
C A:ALA429 3.4 14.5 1.0
CB A:ALA429 3.4 16.4 1.0
N A:VAL430 3.4 14.4 1.0
CB A:MET471 3.5 13.5 1.0
N A:LYS431 3.5 13.2 1.0
C A:VAL430 3.5 14.7 1.0
O A:ALA429 3.5 15.7 1.0
CA A:VAL430 3.5 13.4 1.0
C8 A:0WB701 3.6 13.1 1.0
CE A:MET471 3.6 15.8 1.0
C3 A:0WB701 3.6 12.5 1.0
O A:ILE469 3.7 12.7 1.0
CG1 A:VAL416 4.0 17.1 1.0
CA A:ALA429 4.0 14.8 1.0
O A:VAL430 4.1 15.9 1.0
N A:MET471 4.1 13.4 1.0
C2 A:0WB701 4.1 12.6 1.0
SD A:MET471 4.3 13.8 1.0
CB A:LYS431 4.3 10.8 1.0
CA A:MET471 4.4 12.6 1.0
CG A:MET471 4.4 14.3 1.0
CA A:LYS431 4.4 13.2 1.0
C A:PHE470 4.7 17.4 1.0
C A:ILE469 4.8 12.5 1.0
N9 A:0WB701 4.8 12.2 1.0
N11 A:0WB701 4.9 11.7 1.0
CA A:PHE470 4.9 12.3 1.0
O A:MET471 4.9 13.4 1.0

Reference:

G.De Leon-Boenig, K.K.Bowman, J.A.Feng, T.Crawford, C.Everett, Y.Franke, A.Oh, M.Stanley, S.T.Staben, M.A.Starovasnik, H.J.Wallweber, J.Wu, L.C.Wu, A.R.Johnson, S.G.Hymowitz. The Crystal Structure of the Catalytic Domain of the Nf-Kappab Inducing Kinase Reveals A Narrow But Flexible Active Site. Structure V. 20 1704 2012.
ISSN: ISSN 0969-2126
PubMed: 22921830
DOI: 10.1016/J.STR.2012.07.013
Page generated: Sun Dec 13 12:03:01 2020

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