Atomistry » Zinc » PDB 9baq-9ch1 » 9cgw
Atomistry »
  Zinc »
    PDB 9baq-9ch1 »
      9cgw »

Zinc in PDB 9cgw: Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (No Cofactor)

Protein crystallography data

The structure of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (No Cofactor), PDB code: 9cgw 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) 45.90 / 2.65
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.81, 91.81, 161.17, 90, 90, 120
R / Rfree (%) 22.1 / 28

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (No Cofactor) (pdb code 9cgw). 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 (No Cofactor), PDB code: 9cgw:

Zinc binding site 1 out of 1 in 9cgw

Go back to Zinc Binding Sites List in 9cgw
Zinc binding site 1 out of 1 in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-I65W) Heteromeric Complex (No Cofactor)


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 (No Cofactor) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:79.6
occ:1.00
OE2 C:GLU126 2.2 79.8 1.0
OE2 A:GLU126 2.3 66.2 1.0
NE2 C:HIS142 2.3 49.4 1.0
NE2 A:HIS142 2.3 71.5 1.0
CD2 A:HIS142 2.7 60.2 1.0
CD C:GLU126 3.0 70.6 1.0
CD A:GLU126 3.0 58.6 1.0
OE1 A:GLU126 3.0 56.6 1.0
OE1 C:GLU126 3.1 56.1 1.0
CD2 C:HIS142 3.1 51.2 1.0
CE1 C:HIS142 3.3 49.7 1.0
CE1 A:HIS142 3.6 64.2 1.0
CG A:HIS142 4.0 52.0 1.0
OG C:SER144 4.1 49.8 1.0
CG C:HIS142 4.3 53.5 1.0
ND1 C:HIS142 4.4 52.0 1.0
ND1 A:HIS142 4.4 59.3 1.0
CG C:GLU126 4.4 63.2 1.0
CG A:GLU126 4.5 53.3 1.0
OG A:SER144 4.6 49.1 1.0
CB C:SER144 4.9 50.9 1.0

Reference:

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
Page generated: Sun Feb 9 09:12:19 2025

Last articles

Mn in 4X4O
Mn in 4XJK
Mn in 4XIS
Mn in 4XBW
Mn in 4X9Q
Mn in 4WV8
Mn in 4X8D
Mn in 4WZQ
Mn in 4WZM
Mn in 4WYL
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy