Sodium in PDB 2zoq: Structural Dissection of Human Mitogen-Activated Kinase ERK1

All present enzymatic activity of Structural Dissection of Human Mitogen-Activated Kinase ERK1:
2.7.11.24;

The structure of Structural Dissection of Human Mitogen-Activated Kinase ERK1, PDB code: 2zoq was solved by T.Kinoshita, T.Tada, S.Nakae, I.Yoshida, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.57 / 2.39
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.382, 91.540, 64.930, 90.00, 91.50, 90.00
R / Rfree (%)	n/a / n/a

The structure of Structural Dissection of Human Mitogen-Activated Kinase ERK1 also contains other interesting chemical elements:

Iodine

(I)

2 atoms

The binding sites of Sodium atom in the Structural Dissection of Human Mitogen-Activated Kinase ERK1 (pdb code 2zoq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structural Dissection of Human Mitogen-Activated Kinase ERK1, PDB code: 2zoq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Structural Dissection of Human Mitogen-Activated Kinase ERK1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structural Dissection of Human Mitogen-Activated Kinase ERK1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na381 b:41.8 occ:1.00 OD1 A:ASP184 2.1 20.5 1.0 O A:HOH389 2.6 11.0 1.0 IAE A:5ID382 2.7 38.9 1.0 CG A:ASP184 3.1 17.2 1.0 SG A:CYS183 3.1 15.4 1.0 N A:ASP184 3.6 14.6 1.0 C7 A:5ID382 3.6 30.4 1.0 C8 A:5ID382 3.6 28.1 1.0 OD2 A:ASP184 3.7 17.4 1.0 NZ A:LYS71 3.8 23.5 1.0 CE A:LYS71 3.9 17.5 1.0 CA A:ASP184 4.0 15.2 1.0 CB A:ASP184 4.1 17.9 1.0 O5' A:5ID382 4.3 32.8 1.0 CB A:CYS183 4.3 16.7 1.0 OE1 A:GLN122 4.5 17.4 1.0 C A:CYS183 4.6 13.2 1.0 CA A:CYS183 4.7 15.4 1.0 O A:HOH391 4.9 15.9 1.0 N9 A:5ID382 4.9 26.3 1.0

Sodium binding site 2 out of 2 in the Structural Dissection of Human Mitogen-Activated Kinase ERK1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structural Dissection of Human Mitogen-Activated Kinase ERK1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na381 b:33.0 occ:1.00 OD1 B:ASP184 2.1 19.9 1.0 O B:HOH432 2.8 13.3 1.0 IAE B:5ID382 2.9 33.0 1.0 SG B:CYS183 3.1 11.1 1.0 N B:ASP184 3.1 15.9 1.0 CB B:CYS183 3.2 14.2 1.0 CG B:ASP184 3.3 20.4 1.0 C8 B:5ID382 3.6 25.2 1.0 NZ B:LYS71 3.6 22.5 1.0 C7 B:5ID382 3.6 25.6 1.0 CA B:ASP184 3.7 14.3 1.0 CB B:ASP184 4.0 16.0 1.0 C B:CYS183 4.0 15.2 1.0 CE B:LYS71 4.0 18.8 1.0 CA B:CYS183 4.2 14.0 1.0 OD2 B:ASP184 4.2 25.2 1.0 C5' B:5ID382 4.4 29.2 1.0 O B:HOH518 4.7 40.4 1.0 O5' B:5ID382 4.7 34.8 1.0 N9 B:5ID382 4.8 24.7 1.0 CD B:LYS71 4.8 21.1 1.0 OE1 B:GLN122 4.9 13.1 1.0 C3' B:5ID382 4.9 29.1 1.0 C5 B:5ID382 5.0 25.6 1.0

T.Kinoshita, I.Yoshida, S.Nakae, K.Okita, M.Gouda, M.Matsubara, K.Yokota, H.Ishiguro, T.Tada. Crystal Structure of Human Mono-Phosphorylated ERK1 at TYR204 Biochem.Biophys.Res.Commun. V. 377 1123 2008.
ISSN: ISSN 0006-291X
PubMed: 18983981
DOI: 10.1016/J.BBRC.2008.10.127