Chlorine in PDB 4qtb: Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket

All present enzymatic activity of Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket:
2.7.11.24;

The structure of Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket, PDB code: 4qtb was solved by A.Chaikuad, T.Keates, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, S.Knapp, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.74 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.980, 94.010, 65.360, 90.00, 91.71, 90.00
R / Rfree (%)	14.7 / 17.5

The binding sites of Chlorine atom in the Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket (pdb code 4qtb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket, PDB code: 4qtb:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl416 b:12.0 occ:1.00 N A:ILE273 3.1 11.7 1.0 NE B:ARG94 3.1 12.2 0.5 NE B:ARG94 3.1 13.4 0.5 ND2 A:ASN218 3.3 11.5 1.0 NE2 A:HIS197 3.3 14.1 1.0 N A:ASN274 3.5 10.1 1.0 CB A:ASN218 3.5 9.5 1.0 CD2 A:HIS197 3.7 13.7 1.0 CA A:ILE272 3.7 13.4 1.0 CG A:ASN274 3.7 10.1 1.0 C A:ILE272 3.8 12.6 1.0 CD B:ARG94 3.9 12.3 0.5 CG A:ASN218 3.9 10.8 1.0 ND2 A:ASN274 3.9 10.1 1.0 NH1 B:ARG94 4.0 13.7 0.5 CD B:ARG94 4.0 13.5 0.5 CA A:ILE273 4.0 11.4 0.3 OD1 A:ASN274 4.0 11.1 1.0 CZ B:ARG94 4.0 13.6 0.5 NH1 B:ARG94 4.0 12.3 0.5 CZ B:ARG94 4.0 12.3 0.5 CA A:ILE273 4.1 11.4 0.7 CB A:ASN274 4.1 9.7 1.0 CB A:ILE273 4.1 11.5 0.3 CG2 A:ILE272 4.2 14.4 1.0 C A:ILE273 4.2 11.2 1.0 CG1 A:ILE273 4.2 12.2 0.7 O A:CYS271 4.3 13.6 1.0 CA A:ASN274 4.4 10.0 1.0 CB A:ILE272 4.5 13.8 1.0 CE1 A:HIS197 4.5 14.8 1.0 O B:HOH660 4.6 26.3 1.0 CB A:ILE273 4.7 11.8 0.7 CG1 A:ILE273 4.7 11.5 0.3 N A:ILE272 4.8 12.9 1.0 CG B:ARG94 4.8 12.3 0.5 CG B:ARG94 4.9 13.6 0.5 CA A:ASN218 4.9 9.2 1.0 C A:CYS271 4.9 12.7 1.0 O A:ILE272 5.0 14.8 1.0

Chlorine binding site 2 out of 3 in the Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl409 b:12.1 occ:1.00 N B:ILE273 3.1 11.8 1.0 ND2 B:ASN218 3.3 11.4 1.0 N B:ASN274 3.5 9.9 1.0 CB B:ASN218 3.5 9.9 1.0 CE1 B:HIS197 3.5 15.0 1.0 CA B:ILE272 3.7 12.4 1.0 ND1 B:HIS197 3.7 16.7 1.0 CG B:ASN274 3.8 9.8 1.0 C B:ILE272 3.8 12.9 1.0 CG B:ASN218 3.9 10.9 1.0 OD1 B:ASN274 3.9 10.1 1.0 ND2 B:ASN274 4.0 10.4 1.0 CA B:ILE273 4.1 11.7 1.0 CG1 B:ILE273 4.1 14.1 1.0 CB B:ASN274 4.1 9.7 1.0 CG2 B:ILE272 4.2 13.1 1.0 C B:ILE273 4.2 10.8 1.0 O B:CYS271 4.3 13.2 1.0 CA B:ASN274 4.3 9.9 1.0 CB B:ILE272 4.5 12.8 1.0 CB B:ILE273 4.6 12.9 1.0 NE2 B:HIS197 4.7 17.3 1.0 N B:ILE272 4.8 12.6 1.0 CA B:ASN218 4.9 9.7 1.0 C B:CYS271 5.0 12.6 1.0

Chlorine binding site 3 out of 3 in the Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Human ERK1 in Complex with SCH772984 Revealing A Novel Inhibitor-Induced Binding Pocket within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl410 b:42.2 occ:1.00 N B:GLN79 3.2 12.6 1.0 CD2 B:HIS78 3.3 20.2 0.5 NE2 B:HIS78 3.4 20.4 0.5 CG B:HIS78 3.6 18.2 0.5 CB B:GLN79 3.7 14.3 0.5 CE1 B:HIS78 3.7 18.8 0.5 CB B:GLN79 3.7 13.1 0.5 O B:HOH509 3.7 14.7 1.0 CA B:HIS78 3.8 14.7 0.5 ND1 B:HIS78 3.8 18.9 0.5 CA B:HIS78 3.8 14.6 0.5 C B:HIS78 4.0 13.4 1.0 CD B:LYS357 4.0 16.3 0.5 CA B:GLN79 4.1 12.7 0.5 CA B:GLN79 4.1 12.2 0.5 CD2 B:HIS78 4.2 19.0 0.5 CB B:HIS78 4.3 15.6 0.5 NZ B:LYS357 4.3 17.7 0.5 O B:GLU77 4.3 15.7 1.0 CD B:LYS357 4.4 16.7 0.5 CB B:HIS78 4.4 15.3 0.5 NZ B:LYS357 4.5 18.7 0.5 CE B:LYS357 4.6 17.5 0.5 CG B:HIS78 4.7 17.4 0.5 O B:HOH1031 4.7 42.3 1.0 O B:HOH849 4.8 33.2 1.0 N B:HIS78 4.9 13.9 1.0 CG B:LYS357 4.9 15.0 0.5 CE B:LYS357 4.9 17.7 0.5 CG B:GLN79 5.0 15.8 0.5 CG B:LYS357 5.0 15.2 0.5

A.Chaikuad, E.M C Tacconi, J.Zimmer, Y.Liang, N.S.Gray, M.Tarsounas, S.Knapp. A Unique Inhibitor Binding Site in ERK1/2 Is Associated with Slow Binding Kinetics. Nat.Chem.Biol. V. 10 853 2014.
ISSN: ISSN 1552-4450
PubMed: 25195011
DOI: 10.1038/NCHEMBIO.1629