Sodium in PDB 8w4z: Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent

The structure of Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent, PDB code: 8w4z was solved by M.Tachioka, S.Yamaguchi, A.Nakamura, T.Ishida, K.Kusaka, T.Yamada, N.Yano, T.Chatake, T.Tamada, K.Takeda, S.Niwa, H.Tanaka, S.Takahashi, K.Inaka, N.Furubayashi, S.Deguchi, M.Samejima, K.Igarashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.73, 68.26, 89.77, 90, 90, 90
R / Rfree (%)	22.2 / 24.2

The binding sites of Sodium atom in the Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent (pdb code 8w4z). 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 Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent, PDB code: 8w4z:

Sodium binding site 1 out of 1 in the Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, H2O Solvent within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:16.7 occ:1.00 O A:HOH844 2.2 19.1 1.0 O A:HOH722 2.3 13.8 1.0 O A:HOH643 2.3 13.6 1.0 O4 C:BGC2 2.4 11.5 1.0 O3 C:BGC2 2.8 10.9 1.0 H4 C:BGC2 2.8 15.2 1.0 C4 C:BGC2 3.0 12.7 1.0 C3 C:BGC2 3.5 13.1 1.0 O A:HOH635 3.9 20.0 1.0 O A:HOH842 3.9 23.4 1.0 HZ3 A:TRP360 4.0 18.1 1.0 H3 C:BGC2 4.0 15.7 1.0 O1 A:BGC501 4.1 16.1 1.0 HB2 A:SER176 4.1 16.0 1.0 OG A:SER176 4.1 14.8 1.0 CZ3 A:TRP360 4.2 15.1 1.0 OD2 A:ASP216 4.2 10.6 1.0 HE3 A:TRP360 4.3 15.8 1.0 HB3 A:ASP394 4.3 9.5 1.0 CE3 A:TRP360 4.3 13.2 1.0 O A:HOH655 4.4 17.3 1.0 C5 C:BGC2 4.4 8.8 1.0 H62 C:BGC2 4.5 11.3 1.0 O A:ASP394 4.5 13.4 1.0 OD1 A:ASP170 4.6 11.8 1.0 H2 C:BGC2 4.6 14.8 1.0 O A:HOH621 4.6 11.5 1.0 HB3 A:ALA299 4.6 12.7 1.0 OH A:TYR164 4.6 10.1 1.0 CB A:SER176 4.7 13.3 1.0 H61 C:BGC2 4.7 11.3 1.0 C2 C:BGC2 4.7 12.3 1.0 C6 C:BGC2 4.8 9.4 1.0 H1 A:BGC501 4.8 19.2 1.0 H5 C:BGC2 4.8 10.6 1.0 CH2 A:TRP360 4.8 12.0 1.0 OD2 A:ASP170 4.9 11.4 1.0 HA A:ASP394 5.0 13.4 1.0 HB3 A:ALA175 5.0 15.0 1.0

M.Tachioka, S.Yamaguchi, A.Nakamura, T.Ishida, K.Kusaka, T.Yamada, N.Yano, T.Chatake, T.Tamada, K.Takeda, S.Niwa, H.Tanaka, S.Takahashi, K.Inaka, N.Furubayashi, S.Deguchi, M.Samejima, K.Igarashi. Deprotonated Arginine Controls A Putative Catalytic Base in Invert-Ing Family 6 Glycoside Hydrolase To Be Published.