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Zinc in PDB 9htu: Structure of Endolysin PLYP100 Catalytic Domain

Protein crystallography data

The structure of Structure of Endolysin PLYP100 Catalytic Domain, PDB code: 9htu was solved by E.Scaletti Hutchinson, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.30 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.306, 65.864, 96.512, 90, 90, 90
R / Rfree (%) 15.2 / 18.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Endolysin PLYP100 Catalytic Domain (pdb code 9htu). 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 Structure of Endolysin PLYP100 Catalytic Domain, PDB code: 9htu:

Zinc binding site 1 out of 1 in 9htu

Go back to Zinc Binding Sites List in 9htu
Zinc binding site 1 out of 1 in the Structure of Endolysin PLYP100 Catalytic Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Endolysin PLYP100 Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:16.7
occ:1.00
OD2 A:ASP151 2.0 13.9 1.0
ND1 A:HIS137 2.0 14.6 1.0
ND1 A:HIS28 2.1 13.9 1.0
CG A:ASP151 2.7 14.1 1.0
OD1 A:ASP151 2.8 15.1 1.0
CE1 A:HIS137 3.0 14.7 1.0
CG A:HIS137 3.0 13.1 1.0
CE1 A:HIS28 3.0 13.8 1.0
CG A:HIS28 3.2 13.4 1.0
CB A:HIS137 3.3 14.0 1.0
CB A:HIS28 3.5 13.5 1.0
CA A:HIS28 4.0 13.6 1.0
NE2 A:HIS137 4.1 15.8 1.0
CD2 A:HIS137 4.1 14.3 1.0
CB A:ASP151 4.2 13.4 1.0
NE2 A:HIS28 4.2 13.7 1.0
CD2 A:HIS28 4.2 12.8 1.0
O A:GLU29 4.4 14.0 1.0
N A:GLU29 4.6 13.1 1.0
O A:HOH391 4.6 24.7 1.0
O A:GLY75 4.7 12.8 1.0
CB A:HIS149 4.7 15.3 1.0
CA A:HIS137 4.8 12.7 1.0
OE1 A:GLU89 4.8 16.1 1.0
C A:HIS28 4.9 14.2 1.0

Reference:

K.R.Bateman, E.S.Hutchinson, G.Widmalm, M.J.Miller, P.Stenmark. Structural and Functional Insights Into Listeria Monocytogenes Phage Endolysin PLYP100 - A Promising Food Safety Tool. J.Biol.Chem. 10295 2025.
ISSN: ESSN 1083-351X
PubMed: 40441534
DOI: 10.1016/J.JBC.2025.110295
Page generated: Fri Aug 22 18:06:29 2025

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