Sodium in PDB 8w8v: High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex

The structure of High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex, PDB code: 8w8v 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)	46.10 / 0.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.044, 67.581, 88.354, 90, 90, 90
R / Rfree (%)	n/a / n/a

The structure of High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex (pdb code 8w8v). 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 High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex, PDB code: 8w8v:

Sodium binding site 1 out of 1 in the High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic 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 High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:4.8 occ:1.00 O A:HOH660 2.3 5.0 1.0 O A:HOH894 2.3 7.3 1.0 O A:HOH762 2.3 5.6 1.0 O4 B:BGC3 2.3 4.2 1.0 O3 B:BGC3 2.6 4.7 1.0 C4 B:BGC3 3.0 4.3 1.0 C3 B:BGC3 3.3 4.4 1.0 O A:HOH925 3.6 10.5 0.5 O A:HOH704 3.8 12.4 0.4 O A:HOH633 3.9 5.7 1.0 O1 A:BGC501 3.9 5.6 1.0 O A:HOH925 4.1 6.2 0.5 OG A:SER176 4.1 5.2 1.0 CZ3 A:TRP360 4.2 5.1 1.0 OD2 A:ASP216 4.2 4.0 1.0 CE3 A:TRP360 4.2 4.7 1.0 O A:HOH731 4.3 5.2 1.0 C5 B:BGC3 4.4 3.9 1.0 OD1 A:ASP170 4.5 4.2 1.0 O A:ASP394 4.5 4.9 1.0 OH A:TYR164 4.6 4.3 1.0 C2 B:BGC3 4.6 4.5 1.0 CB A:SER176 4.6 4.6 1.0 O A:HOH627 4.7 4.3 1.0 CH2 A:TRP360 4.9 5.4 1.0 C6 B:BGC3 4.9 4.4 1.0 OD2 A:ASP170 5.0 4.7 1.0 CD2 A:TRP360 5.0 4.3 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.