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Potassium in PDB 4cgb: Crystal Structure of the Trimerization Domain of EML2

Protein crystallography data

The structure of Crystal Structure of the Trimerization Domain of EML2, PDB code: 4cgb was solved by M.W.Richards, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.846 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.871, 51.135, 101.691, 90.00, 90.00, 90.00
R / Rfree (%) 20.55 / 25.15

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Trimerization Domain of EML2 (pdb code 4cgb). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Trimerization Domain of EML2, PDB code: 4cgb:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 4cgb

Go back to Potassium Binding Sites List in 4cgb
Potassium binding site 1 out of 2 in the Crystal Structure of the Trimerization Domain of EML2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Trimerization Domain of EML2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1001

b:48.0
occ:1.00
O A:HOH2010 3.7 53.7 1.0
O C:HOH2007 3.8 51.9 1.0
CG1 C:VAL35 4.1 43.3 1.0
CA C:LEU36 4.2 29.8 1.0
N C:LEU36 4.4 30.6 1.0
CD1 C:LEU36 4.5 46.8 1.0
CB C:ALA39 4.5 24.6 1.0
CD2 A:LEU40 4.5 28.2 1.0
CB C:LEU36 4.6 28.4 1.0
C C:VAL35 4.7 26.0 1.0
O C:VAL35 4.7 30.8 1.0
CE A:LYS37 4.9 42.8 0.5
CG A:LYS37 5.0 33.4 0.5
CG C:LEU36 5.0 40.3 1.0

Potassium binding site 2 out of 2 in 4cgb

Go back to Potassium Binding Sites List in 4cgb
Potassium binding site 2 out of 2 in the Crystal Structure of the Trimerization Domain of EML2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Trimerization Domain of EML2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1001

b:36.7
occ:1.00
O E:HOH2007 3.7 46.3 1.0
CA D:LEU36 4.0 30.1 1.0
CG1 D:VAL35 4.0 32.5 1.0
CD1 D:LEU36 4.3 43.0 1.0
N D:LEU36 4.3 29.7 1.0
O D:VAL35 4.4 30.6 1.0
CB D:LEU36 4.4 28.8 1.0
CG E:LYS37 4.5 33.2 1.0
C D:VAL35 4.5 27.0 1.0
CB D:ALA39 4.6 24.0 1.0
CD E:LYS37 4.8 44.5 1.0
O E:HOH2003 4.8 36.7 1.0
CD2 E:LEU40 4.9 27.2 1.0
CG D:LEU36 4.9 39.9 1.0
CB E:LYS37 4.9 23.7 1.0

Reference:

M.W.Richards, L.O'regan, D.Roth, J.M.Montgomery, E.W.P.Law, S.Busacca, D.A.Fennell, A.Straube, A.M.Fry, R.Bayliss. Microtubule Association of Eml Proteins and the EML4-Alk Variant 3 Oncoprotein Require An N- Terminal Trimerization Domain To Be Published.
Page generated: Mon Aug 12 10:24:18 2024

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