Chlorine in PDB 4fv2: Crystal Structure of the ERK2 Complexed with EK5

All present enzymatic activity of Crystal Structure of the ERK2 Complexed with EK5:
2.7.11.24;

The structure of Crystal Structure of the ERK2 Complexed with EK5, PDB code: 4fv2 was solved by Y.N.Kang, J.A.Stuckey, X.Xie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.18 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.620, 70.310, 60.230, 90.00, 109.46, 90.00
R / Rfree (%)	17.9 / 21.1

The binding sites of Chlorine atom in the Crystal Structure of the ERK2 Complexed with EK5 (pdb code 4fv2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the ERK2 Complexed with EK5, PDB code: 4fv2:

Chlorine binding site 1 out of 1 in the Crystal Structure of the ERK2 Complexed with EK5


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 the ERK2 Complexed with EK5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:51.7 occ:1.00 CL A:EK5401 0.0 51.7 1.0 C1 A:EK5401 1.7 47.9 1.0 C2 A:EK5401 2.7 45.7 1.0 C6 A:EK5401 2.7 48.2 1.0 H3 A:EK5401 2.8 45.6 1.0 H6 A:EK5401 2.8 48.5 1.0 H19 A:EK5401 2.9 35.6 1.0 C A:GLY30 3.4 59.5 1.0 CG2 A:VAL37 3.5 48.9 1.0 N A:GLU31 3.6 56.2 1.0 CA A:GLY30 3.6 55.9 1.0 O A:GLY30 3.7 58.9 1.0 H18 A:EK5401 3.7 36.7 1.0 O A:HOH674 3.8 44.3 1.0 CB A:VAL37 3.8 49.9 1.0 C23 A:EK5401 3.9 35.7 1.0 C5 A:EK5401 4.0 47.7 1.0 C3 A:EK5401 4.0 43.8 1.0 H8 A:EK5401 4.1 34.8 1.0 N A:GLY30 4.2 55.9 1.0 CA A:GLU31 4.2 56.2 1.0 C22 A:EK5401 4.2 36.8 1.0 H10 A:EK5401 4.4 35.2 1.0 C4 A:EK5401 4.5 46.2 1.0 O A:GLU31 4.6 60.0 1.0 C A:GLU31 4.6 59.9 1.0 C11 A:EK5401 4.7 35.3 1.0 CG1 A:VAL37 4.7 49.3 1.0 H5 A:EK5401 4.8 47.8 1.0 N A:VAL37 4.8 48.4 1.0 N4 A:EK5401 4.9 35.2 1.0 CA A:VAL37 4.9 47.4 1.0

Y.N.Kang, J.A.Stuckey, X.Xie. Crystal Structure of the ERK2 Complexed with EK5 To Be Published.