Sodium in PDB 8w4x: Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex

The structure of Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex, PDB code: 8w4x 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 / 1.40
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 (%)	14.7 / 16.6

The binding sites of Sodium atom in the Neutron Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Room Temperature, Enzyme-Product Complex (pdb code 8w4x). 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, PDB code: 8w4x:

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:10.4 occ:1.00 O A:HOH847 2.2 16.8 1.0 O A:HOH667 2.3 10.4 1.0 O4 C:BGC2 2.3 7.7 1.0 O A:HOH719 2.4 11.4 1.0 O3 C:BGC2 2.7 8.5 1.0 DO4 C:BGC2 2.8 9.3 0.6 D1 A:HOH719 2.9 13.6 0.5 H4 C:BGC2 3.0 8.6 1.0 HO4 C:BGC2 3.0 9.3 0.4 C4 C:BGC2 3.1 7.1 1.0 C3 C:BGC2 3.5 6.3 1.0 DO3 C:BGC2 3.5 10.2 0.6 DG A:SER176 3.5 12.6 0.6 HG A:SER176 3.5 12.6 0.4 HO3 C:BGC2 3.6 10.2 0.4 O A:HOH630 3.8 12.5 1.0 O A:HOH610 3.8 23.3 0.7 O1 A:BGC501 4.0 11.1 1.0 HZ3 A:TRP360 4.0 11.5 1.0 H3 C:BGC2 4.0 7.6 1.0 O A:HOH843 4.0 17.6 1.0 HB2 A:SER176 4.1 10.4 1.0 OG A:SER176 4.1 10.5 1.0 CZ3 A:TRP360 4.2 9.6 1.0 OD2 A:ASP216 4.3 7.4 1.0 HE3 A:TRP360 4.3 10.2 1.0 HB3 A:ASP394 4.3 8.6 1.0 CE3 A:TRP360 4.3 8.5 1.0 DH A:TYR164 4.3 9.7 0.6 HH A:TYR164 4.4 9.7 0.5 O A:HOH664 4.4 11.5 1.0 C5 C:BGC2 4.5 6.7 1.0 OD1 A:ASP170 4.5 7.0 1.0 O A:ASP394 4.5 9.4 1.0 H62 C:BGC2 4.6 9.9 1.0 CB A:SER176 4.6 8.7 1.0 H2 C:BGC2 4.6 8.6 1.0 OH A:TYR164 4.7 8.1 1.0 O A:HOH620 4.7 7.1 1.0 D2 A:HOH731 4.7 12.1 0.3 C2 C:BGC2 4.7 7.2 1.0 H61 C:BGC2 4.8 9.9 1.0 HB2 A:ALA299 4.8 7.7 1.0 CH2 A:TRP360 4.9 9.6 1.0 OD2 A:ASP170 4.9 9.4 1.0 H5 C:BGC2 4.9 8.0 1.0 C6 C:BGC2 4.9 8.3 1.0 HA A:ASP394 4.9 7.9 1.0 H1 A:BGC501 5.0 10.5 1.0 CG A:ASP170 5.0 8.1 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.