Sodium in PDB 7soi: Structure of I552A Soybean Lipoxygenase at 277K

The structure of Structure of I552A Soybean Lipoxygenase at 277K, PDB code: 7soi was solved by C.L.Gee, A.R.Offenbacher, S.Hu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.38 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	91.531, 92.759, 99.836, 90, 93.56, 90
R / Rfree (%)	19.8 / 25.9

The structure of Structure of I552A Soybean Lipoxygenase at 277K also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Sodium atom in the Structure of I552A Soybean Lipoxygenase at 277K (pdb code 7soi). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of I552A Soybean Lipoxygenase at 277K, PDB code: 7soi:

Sodium binding site 1 out of 1 in the Structure of I552A Soybean Lipoxygenase at 277K


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of I552A Soybean Lipoxygenase at 277K within 5.0Å range: probe atom residue distance (Å) B Occ B:Na902 b:76.3 occ:1.00 OG1 B:THR623 2.3 70.7 1.0 HG21 B:THR623 2.8 55.1 1.0 HG1 B:THR623 2.8 84.8 1.0 HB B:THR623 3.0 60.1 1.0 CB B:THR623 3.0 50.1 1.0 HD3 B:LYS788 3.2 77.3 1.0 CG2 B:THR623 3.3 45.9 1.0 HG2 B:LYS788 3.5 71.9 1.0 HZ2 B:LYS784 3.7 114.7 1.0 HZ1 B:LYS784 3.7 114.7 1.0 HG23 B:THR623 3.8 55.1 1.0 HA B:ALA620 3.9 48.0 1.0 NZ B:LYS784 4.0 95.6 1.0 HZ3 B:LYS784 4.0 114.7 1.0 CD B:LYS788 4.1 64.4 1.0 HG22 B:THR623 4.1 55.1 1.0 CG B:LYS788 4.2 59.9 1.0 HB2 B:LYS788 4.3 54.9 1.0 CA B:THR623 4.4 43.7 1.0 HD2 B:LYS788 4.6 77.3 1.0 H B:THR623 4.7 41.3 1.0 CB B:LYS788 4.7 45.7 1.0 O B:ALA620 4.7 39.5 1.0 HB3 B:LYS788 4.8 54.9 1.0 HZ2 B:LYS788 4.8 121.1 1.0 CA B:ALA620 4.8 40.0 1.0 O B:ALA619 4.9 40.6 1.0 C B:THR623 4.9 54.4 1.0 HE2 B:LYS788 5.0 70.2 1.0

J.P.T.Zaragoza, A.R.Offenbacher, S.Hu, C.L.Gee, Z.M.Firestein, N.Minnetian, Z.Deng, A.T.Iavarone, J.P.Klinman. A Dynamically-Activated Protein Quake Controls the Thermal Activation of Enzyme Catalyzed Hydrogen Tunneling To Be Published.