Iodine in PDB 6kwd: Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose

All present enzymatic activity of Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose:
3.2.1.8;

The structure of Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose, PDB code: 6kwd was solved by C.Li, Q.Wan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.73 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.598, 59.161, 69.604, 90, 90, 90
R / Rfree (%)	15.1 / 16.3

The binding sites of Iodine atom in the Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose (pdb code 6kwd). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose, PDB code: 6kwd:

Iodine binding site 1 out of 1 in the Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure Analysis of Endo-Beta-1,4-Xylanase II Complexed with Xylotriose within 5.0Å range: probe atom residue distance (Å) B Occ A:I202 b:16.5 occ:1.00 H A:SER146 2.7 17.5 1.0 HG A:SER146 3.2 19.0 0.6 HB2 A:ARG145 3.4 18.9 1.0 HA A:ARG145 3.4 18.4 1.0 O A:HOH374 3.5 20.9 1.0 N A:SER146 3.6 14.6 1.0 O A:HOH337 3.6 16.5 1.0 H A:SER147 3.7 18.7 1.0 OG A:SER146 3.8 15.8 0.6 CA A:ARG145 4.1 15.3 1.0 O A:HOH308 4.1 29.4 1.0 CB A:ARG145 4.1 15.8 1.0 HB2 A:SER146 4.2 20.0 0.4 N A:SER147 4.3 15.6 1.0 HB2 A:SER147 4.4 18.5 1.0 HB3 A:ARG145 4.4 18.9 1.0 HG A:SER146 4.4 19.6 0.4 C A:ARG145 4.4 13.9 1.0 CA A:SER146 4.5 15.1 1.0 HG A:SER147 4.6 19.9 1.0 O A:HOH524 4.6 30.7 1.0 C A:SER146 4.7 16.0 1.0 CB A:SER146 4.7 16.7 1.0 OG A:SER146 5.0 16.4 0.4

Z.Li, X.Zhang, C.Li, A.Kovalevsky, Q.Wan. Studying the Role of A Single Mutation of A Family 11 Glycoside Hydrolase Using High-Resolution X-Ray Crystallography. Protein J. V. 39 671 2020.
ISSN: ISSN 1572-3887
PubMed: 33128114
DOI: 10.1007/S10930-020-09938-5