Chlorine 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:

Sodium

(Na)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the High-Resolution X-Ray Structure of Cellulase CEL6A From Phanerochaete Chrysosporium at Cryogenic Temperature, Enzyme-Product Complex, PDB code: 8w8v:

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl503 b:8.3 occ:1.00 O A:HOH935 3.2 5.9 0.4 N A:GLN228 3.2 5.9 1.0 O A:HOH935 3.3 9.8 0.6 O A:HOH1113 3.5 52.2 1.0 O A:ASN226 3.7 8.7 0.3 CG A:GLN228 3.8 8.7 1.0 CA A:VAL227 3.9 5.7 1.0 CB A:GLN228 3.9 8.5 1.0 C A:VAL227 4.0 5.2 1.0 O A:ASN226 4.1 6.1 0.7 CA A:GLN228 4.2 6.7 1.0 O A:HOH1139 4.3 38.5 1.0 CG1 A:VAL227 4.5 8.4 1.0 C A:ASN226 4.7 7.0 0.3 CB A:VAL227 4.8 6.5 1.0 N A:VAL227 4.9 5.8 1.0 C A:ASN226 4.9 5.4 0.7 CD A:GLN228 4.9 9.5 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.