Zinc in PDB 6enx: Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10

The structure of Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10, PDB code: 6enx was solved by M.Pannek, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.11 / 1.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.470, 38.250, 75.550, 90.00, 122.51, 90.00
R / Rfree (%)	19.5 / 24.2

The binding sites of Zinc atom in the Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10 (pdb code 6enx). 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 Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10, PDB code: 6enx:

Zinc binding site 1 out of 1 in the Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zebrafish SIRT5 in Complex with Stalled Bicyclic Intermediate of Inhibitory Compound 10 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:29.9 occ:1.00 SG A:CYS203 2.3 26.3 1.0 SG A:CYS208 2.3 28.1 1.0 SG A:CYS165 2.3 30.9 1.0 SG A:CYS162 2.3 28.4 1.0 CB A:CYS203 3.1 28.4 1.0 CB A:CYS162 3.2 26.3 1.0 CB A:CYS165 3.2 31.0 1.0 CB A:CYS208 3.3 30.8 1.0 N A:CYS165 3.9 34.3 1.0 CA A:CYS165 4.1 30.8 1.0 N A:GLY210 4.5 30.8 1.0 CA A:CYS203 4.5 28.9 1.0 CB A:ARG205 4.6 45.9 1.0 CA A:CYS162 4.7 26.5 1.0 CA A:CYS208 4.7 33.4 1.0 O A:HOH548 4.7 33.0 1.0 CB A:GLU167 4.7 34.6 1.0 CB A:SER164 4.8 34.6 1.0 C A:CYS165 4.8 30.1 1.0 CA A:GLY210 4.9 25.7 1.0 N A:GLY166 4.9 28.0 1.0 CD A:ARG205 4.9 42.1 1.0 O A:HOH545 5.0 41.9 1.0

N.Rajabi, M.Auth, K.R.Troelsen, M.Pannek, D.P.Bhatt, M.Fontenas, M.D.Hirschey, C.Steegborn, A.S.Madsen, C.A.Olsen. Mechanism-Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure-Activity Relationship, Biostructural, and Kinetic Insight. Angew. Chem. Int. Ed. Engl. V. 56 14836 2017.
ISSN: ESSN 1521-3773
PubMed: 29044784
DOI: 10.1002/ANIE.201709050