Chlorine in PDB 4fv7: Crystal Structure of the ERK2 Complexed with E94

All present enzymatic activity of Crystal Structure of the ERK2 Complexed with E94:
2.7.11.24;

The structure of Crystal Structure of the ERK2 Complexed with E94, PDB code: 4fv7 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)	27.10 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.630, 70.190, 61.120, 90.00, 111.20, 90.00
R / Rfree (%)	18.3 / 20.8

The binding sites of Chlorine atom in the Crystal Structure of the ERK2 Complexed with E94 (pdb code 4fv7). 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 E94, PDB code: 4fv7:

Chlorine binding site 1 out of 1 in the Crystal Structure of the ERK2 Complexed with E94


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 E94 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:33.6 occ:1.00 CL A:E94401 0.0 33.6 1.0 C1 A:E94401 1.7 33.5 1.0 C2 A:E94401 2.7 32.1 1.0 C6 A:E94401 2.7 32.4 1.0 H2 A:E94401 2.8 32.1 0.0 H5 A:E94401 2.8 32.4 0.0 OE2 A:GLU69 3.3 34.2 1.0 O A:HOH653 3.6 28.2 1.0 O A:HOH590 3.6 29.3 1.0 CD1 A:LEU73 3.6 30.8 1.0 CG2 A:ILE101 3.6 27.2 1.0 OE1 A:GLN103 3.7 35.3 1.0 CD A:GLN103 3.9 41.7 1.0 CD A:LYS52 3.9 35.7 1.0 C5 A:E94401 4.0 31.8 1.0 C3 A:E94401 4.0 31.5 1.0 NE2 A:GLN103 4.0 36.1 1.0 CB A:ILE101 4.1 27.7 1.0 CD1 A:ILE101 4.2 32.4 1.0 CD A:GLU69 4.4 39.1 1.0 NZ A:LYS52 4.5 34.4 1.0 C4 A:E94401 4.5 32.6 1.0 CG A:GLN103 4.5 28.2 1.0 CB A:LYS52 4.6 28.8 1.0 CG1 A:ILE101 4.7 28.3 1.0 CE A:LYS52 4.8 36.7 1.0 N3 A:E94401 4.8 32.7 1.0 H4 A:E94401 4.8 31.8 0.0 CG A:LYS52 4.9 31.5 1.0 C18 A:E94401 5.0 31.7 1.0

Y.N.Kang, J.A.Stuckey, X.Xie. Crystal Structure of the ERK2 Complexed with E94 To Be Published.