Zinc in PDB 8k7x: Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris

Enzymatic activity of Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris

All present enzymatic activity of Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris:
3.2.1.185;

Protein crystallography data

The structure of Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris, PDB code: 8k7x was solved by L.Pan, S.Maruyama, M.Miyake, K.Fujita, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.76 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.592, 111.571, 153.01, 90, 90, 90
R / Rfree (%) 14.3 / 16.7

Other elements in 8k7x:

The structure of Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris (pdb code 8k7x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris, PDB code: 8k7x:

Zinc binding site 1 out of 1 in 8k7x

Go back to Zinc Binding Sites List in 8k7x
Zinc binding site 1 out of 1 in the Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of GH146 Beta-L-Arabinofuranosidase BLL3HYPBA1 (Amino Acids 380-1223) in Complex with Tris within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1301

b:9.2
occ:1.00
 OE2 A:GLU723 2.0 7.6 1.0
SG A:CYS805 2.3 8.2 1.0
SG A:CYS725 2.3 8.3 1.0
SG A:CYS804 2.4 9.8 1.0
CD A:GLU723 3.0 8.3 1.0
N A:CYS805 3.2 7.6 1.0
CB A:CYS725 3.2 7.3 1.0
CG A:GLU723 3.3 7.7 1.0
CB A:CYS804 3.4 8.5 1.0
CB A:CYS805 3.5 8.1 1.0
CA A:CYS805 3.5 8.1 1.0
C A:CYS804 3.7 7.5 1.0
N A:CYS725 3.9 6.1 1.0
CA A:CYS804 4.1 7.8 1.0
CZ A:TYR771 4.1 7.4 1.0
CA A:CYS725 4.1 6.7 1.0
OE1 A:GLU723 4.2 8.6 1.0
CE2 A:TYR771 4.2 7.1 1.0
N A:TRS1302 4.2 22.2 1.0
OH A:TYR771 4.2 8.2 1.0
O A:CYS804 4.5 7.0 1.0
CE1 A:TYR771 4.5 7.8 1.0
CD2 A:TYR771 4.7 6.9 1.0
N A:CYS804 4.7 7.7 1.0
CB A:GLU723 4.9 7.4 1.0
ND2 A:ASN630 4.9 8.8 1.0
O A:HOH1552 4.9 9.4 1.0
CD1 A:TYR771 5.0 7.1 1.0

Reference:

K.Fujita, H.Tsunomachi, P.Lixia, S.Maruyama, M.Miyake, A.Dakeshita, K.Kitahara, K.Tanaka, Y.Ito, A.Ishiwata, S.Fushinobu. Bifidobacterial GH146 Beta-L-Arabinofuranosidase For the Removal of Beta 1,3-L-Arabinofuranosides on Plant Glycans. Appl.Microbiol.Biotechnol. V. 108 199 2024.
ISSN: ESSN 1432-0614
PubMed: 38324037
DOI: 10.1007/S00253-024-13014-8
Page generated: Thu Oct 31 08:37:51 2024

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