Zinc in PDB 9ch1: Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam)

The structure of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam), PDB code: 9ch1 was solved by K.K.Crone, J.W.Labonte, M.Elias, M.F.Freeman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.22 / 2.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.2, 59.1, 59.3, 96, 112.4, 93.4
R / Rfree (%)	21 / 24.9

The binding sites of Zinc atom in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam) (pdb code 9ch1). 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 the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam), PDB code: 9ch1:

Zinc binding site 1 out of 1 in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (Bound to Sam) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:33.7 occ:0.60 OE2 C:GLU126 2.0 40.5 1.0 CE1 A:HIS142 2.0 44.3 1.0 OE2 A:GLU126 2.1 47.3 1.0 NE2 C:HIS142 2.2 32.7 1.0 CD A:GLU126 2.8 36.8 1.0 CD C:GLU126 2.9 39.8 1.0 CE1 C:HIS142 2.9 33.0 1.0 ND1 A:HIS142 2.9 40.8 1.0 OE1 A:GLU126 2.9 46.3 1.0 NE2 A:HIS142 3.1 42.3 1.0 OE1 C:GLU126 3.2 43.8 1.0 CD2 C:HIS142 3.4 32.6 1.0 ND1 C:HIS142 4.1 32.4 1.0 CG A:HIS142 4.1 39.0 1.0 CG C:GLU126 4.1 37.8 1.0 CG A:GLU126 4.2 34.4 1.0 CD2 A:HIS142 4.2 43.9 1.0 CG C:HIS142 4.3 31.4 1.0 OG A:SER144 4.6 26.4 1.0 OG C:SER144 4.7 23.2 1.0

K.K.Crone, J.W.Labonte, M.H.Elias, M.F.Freeman. Alpha-N-Methyltransferase Regiospecificity Is Mediated By Proximal, Redundant Enzyme-Substrate Interactions. Protein Sci. V. 34 70021 2025.
ISSN: ESSN 1469-896X
PubMed: 39840790
DOI: 10.1002/PRO.70021