Chlorine in PDB 9eu1: GH29A Alpha-L-Fucosidase

The structure of GH29A Alpha-L-Fucosidase, PDB code: 9eu1 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)	40.67 / 1.92
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	139.167, 139.167, 110.233, 90, 90, 120
R / Rfree (%)	18.3 / 21.4

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

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the GH29A Alpha-L-Fucosidase (pdb code 9eu1). 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: 9eu1:

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:Cl504 b:51.4 occ:1.00 H A:ALA358 2.5 44.8 1.0 HE1 A:HIS360 3.0 47.3 1.0 HG13 A:VAL357 3.1 45.7 1.0 HB3 A:ALA358 3.2 47.6 1.0 HA A:VAL357 3.2 44.8 1.0 HG2 A:PRO387 3.3 48.6 1.0 N A:ALA358 3.3 37.2 1.0 HG3 A:PRO387 3.5 48.6 1.0 HB2 A:ALA358 3.7 47.6 1.0 CB A:ALA358 3.8 39.6 1.0 CG A:PRO387 3.9 40.4 1.0 CE1 A:HIS360 3.9 39.3 1.0 CA A:VAL357 4.0 37.3 1.0 CG1 A:VAL357 4.0 38.0 1.0 CA A:ALA358 4.1 37.2 1.0 C A:VAL357 4.2 37.2 1.0 HG12 A:VAL357 4.3 45.7 1.0 HG22 A:VAL357 4.5 46.5 1.0 O A:LEU356 4.5 39.3 1.0 CB A:VAL357 4.6 37.4 1.0 O A:ALA358 4.6 35.2 1.0 HB1 A:ALA358 4.7 47.6 1.0 HG11 A:VAL357 4.7 45.7 1.0 NE2 A:HIS360 4.7 38.6 1.0 HB2 A:PRO387 4.8 47.4 1.0 HD2 A:PRO387 4.8 47.3 1.0 C A:ALA358 4.9 36.5 1.0 ND1 A:HIS360 4.9 37.9 1.0 HD1 A:HIS360 4.9 45.5 1.0 CB A:PRO387 4.9 39.4 1.0 HA A:ALA358 4.9 44.8 1.0 CD A:PRO387 5.0 39.3 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