Chlorine in PDB 9eu3: GH29A Alpha-L-Fucosidase

All present enzymatic activity of GH29A Alpha-L-Fucosidase:
3.2.1.51;

The structure of GH29A Alpha-L-Fucosidase, PDB code: 9eu3 was solved by Y.Y.Yang, B.Zeuner, J.P.Morth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.28 / 2.28
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	146.871, 146.871, 196.703, 90, 90, 120
R / Rfree (%)	21.2 / 24.3

The structure of GH29A Alpha-L-Fucosidase also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the GH29A Alpha-L-Fucosidase (pdb code 9eu3). 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 GH29A Alpha-L-Fucosidase, PDB code: 9eu3:

Chlorine binding site 1 out of 1 in the GH29A Alpha-L-Fucosidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of GH29A Alpha-L-Fucosidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:77.2 occ:1.00 HG1 A:THR358 2.1 82.2 1.0 HE3 A:LYS43 2.5 68.4 1.0 HE2 A:LYS43 2.7 68.4 1.0 HA A:ARG359 2.8 74.2 1.0 OG1 A:THR358 2.8 67.8 1.0 HG22 A:THR372 2.9 74.6 1.0 O A:ALA315 3.0 56.6 1.0 CE A:LYS43 3.0 56.2 1.0 HB1 A:ALA315 3.0 73.2 1.0 C A:ARG359 3.1 59.9 1.0 CA A:ARG359 3.2 61.1 1.0 N A:ARG359 3.2 65.1 1.0 O A:ARG359 3.3 62.4 1.0 C A:THR358 3.3 66.2 1.0 O A:THR358 3.3 63.0 1.0 HG21 A:THR372 3.4 74.6 1.0 CG2 A:THR372 3.5 61.4 1.0 N A:GLY360 3.6 58.7 1.0 HA A:ALA315 3.6 69.2 1.0 HZ1 A:LYS43 3.6 68.3 1.0 HB A:THR372 3.7 76.1 1.0 H A:ARG359 3.7 79.0 1.0 C A:ALA315 3.7 56.0 1.0 H A:GLY360 3.8 71.3 1.0 CB A:THR358 3.8 68.1 1.0 CB A:ALA315 3.9 60.2 1.0 HA A:ASN318 3.9 71.6 1.0 NZ A:LYS43 3.9 56.2 1.0 HB A:THR358 3.9 82.6 1.0 CA A:ALA315 3.9 56.9 1.0 HA2 A:GLY360 4.0 69.2 1.0 O A:ILE355 4.1 71.2 0.7 HD2 A:LYS43 4.1 67.9 1.0 CA A:THR358 4.1 67.4 1.0 CB A:THR372 4.1 62.7 1.0 O A:ILE355 4.2 71.1 0.3 CD A:LYS43 4.2 55.9 1.0 HG23 A:THR372 4.3 74.6 1.0 HG3 A:LYS43 4.3 69.3 1.0 CA A:GLY360 4.3 56.9 1.0 HB2 A:ALA315 4.4 73.2 1.0 HZ2 A:LYS43 4.4 68.3 1.0 HA A:THR372 4.4 76.3 1.0 H A:THR358 4.5 82.8 1.0 HB3 A:ALA315 4.5 73.2 1.0 H A:ASN318 4.5 68.1 1.0 HA A:ILE355 4.5 59.7 0.3 HZ3 A:LYS43 4.5 68.3 1.0 H A:GLN373 4.6 78.0 1.0 CB A:ARG359 4.7 59.1 1.0 OD1 A:ASN318 4.7 58.8 1.0 HD3 A:ARG359 4.7 73.8 1.0 CG A:LYS43 4.7 57.0 1.0 HA A:ILE355 4.8 84.4 0.7 CA A:ASN318 4.8 58.9 1.0 N A:THR358 4.8 68.3 1.0 HG2 A:LYS43 4.9 69.3 1.0 N A:GLY316 4.9 54.8 1.0 HA2 A:GLY316 4.9 65.2 1.0 CA A:THR372 4.9 62.9 1.0 HA A:THR358 4.9 81.8 1.0 HD3 A:LYS43 4.9 67.9 1.0 HB3 A:ARG359 4.9 71.8 1.0 O A:HOH601 5.0 58.2 1.0

Y.Yang, J.Holck, A.T.Thorhallsson, C.J.Hunt, H.Yang, J.P.Morth, A.S.Meyer, B.Zeuner. Structural Elucidation and Characterization of GH29A Alpha-L-Fucosidases and the Effect of pH on Their Transglycosylation. Febs J. V. 292 653 2025.
ISSN: ISSN 1742-464X
PubMed: 39658312
DOI: 10.1111/FEBS.17347