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Bromine in PDB 1s9j: X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp

Enzymatic activity of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp

All present enzymatic activity of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp:
2.7.1.37;

Protein crystallography data

The structure of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp, PDB code: 1s9j was solved by J.F.Ohren, H.Chen, A.Pavlovsky, C.Whitehead, C.Yan, P.Mcconnell, A.Delaney, D.T.Dudley, J.Sebolt-Leopold, C.A.Hasemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.70 / 2.40
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 81.591, 81.591, 129.213, 90.00, 90.00, 120.00
R / Rfree (%) 24.5 / 26.9

Other elements in 1s9j:

The structure of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 1 atom
Iodine (I) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp (pdb code 1s9j). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp, PDB code: 1s9j:

Bromine binding site 1 out of 1 in 1s9j

Go back to Bromine Binding Sites List in 1s9j
Bromine binding site 1 out of 1 in the X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of X-Ray Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) in A Complex with Ligand and Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1001

b:74.0
occ:1.00
 BR A:BBM1001 0.0 74.0 1.0
C10 A:BBM1001 1.9 72.4 1.0
C9 A:BBM1001 2.8 64.5 1.0
C11 A:BBM1001 2.9 78.3 1.0
O A:HOH1105 2.9 34.7 1.0
F1 A:BBM1001 3.1 0.2 1.0
CG1 A:ILE216 3.4 26.4 1.0
CE A:MET219 4.0 35.2 1.0
CA A:ILE216 4.1 26.6 1.0
N A:ILE216 4.1 25.6 1.0
C8 A:BBM1001 4.2 57.8 1.0
CA A:GLY210 4.2 10.4 1.0
C12 A:BBM1001 4.3 68.4 1.0
CB A:ILE216 4.4 26.6 1.0
C A:LEU215 4.5 24.5 1.0
CD1 A:ILE216 4.5 26.2 1.0
O A:PHE209 4.6 8.7 1.0
O A:LEU215 4.7 24.4 1.0
CB A:LEU215 4.7 23.7 1.0
O A:SER212 4.8 16.3 1.0
N A:GLY210 4.8 9.5 1.0
C13 A:BBM1001 4.8 59.3 1.0
C A:PHE209 4.9 8.5 1.0

Reference:

J.F.Ohren, H.Chen, A.Pavlovsky, C.Whitehead, E.Zhang, P.Kuffa, C.Yan, P.Mcconnell, C.Spessard, C.Banotai, W.T.Mueller, A.Delaney, C.Omer, J.Sebolt-Leopold, D.T.Dudley, I.K.Leung, C.Flamme, J.Warmus, M.Kaufman, S.Barrett, H.Tecle, C.A.Hasemann. Structures of Human Map Kinase Kinase 1 (MEK1) and MEK2 Describe Novel Noncompetitive Kinase Inhibition. Nat.Struct.Mol.Biol. V. 11 1192 2004.
ISSN: ISSN 1545-9993
PubMed: 15543157
DOI: 10.1038/NSMB859
Page generated: Wed Jul 10 17:19:19 2024

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