Sodium in PDB 7rc2: Aeronamide N-Methyltransferase, Aere

The structure of Aeronamide N-Methyltransferase, Aere, PDB code: 7rc2 was solved by D.P.Cogan, R.Reyes, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.50 / 1.51
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.566, 77.566, 152.314, 90, 90, 120
R / Rfree (%)	16.1 / 17.5

The structure of Aeronamide N-Methyltransferase, Aere also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Sodium atom in the Aeronamide N-Methyltransferase, Aere (pdb code 7rc2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Aeronamide N-Methyltransferase, Aere, PDB code: 7rc2:

Sodium binding site 1 out of 1 in the Aeronamide N-Methyltransferase, Aere


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Aeronamide N-Methyltransferase, Aere within 5.0Å range: probe atom residue distance (Å) B Occ A:Na403 b:17.2 occ:1.00 O A:HOH564 2.4 32.5 1.0 O A:PRO232 2.4 15.9 1.0 OD1 A:ASN231 2.5 15.7 1.0 O A:HOH553 2.6 21.6 1.0 O A:HOH763 2.7 20.0 1.0 CE2 A:PHE234 3.1 16.3 1.0 CD2 A:PHE234 3.2 14.6 1.0 C A:PRO232 3.3 14.7 1.0 CG A:ASN231 3.4 16.0 1.0 O A:ASN231 3.7 15.4 1.0 CZ A:PHE234 3.9 17.0 1.0 C A:ASN231 3.9 15.2 1.0 N A:PRO233 3.9 15.3 1.0 ND2 A:ASN231 4.0 14.8 1.0 CA A:PRO233 4.0 14.6 1.0 CG A:PHE234 4.1 15.9 1.0 N A:PRO232 4.1 13.0 1.0 O A:TYR246 4.2 18.8 1.0 O A:HOH1000 4.2 26.4 1.0 SD A:SAH401 4.3 18.1 1.0 OD2 A:ASP141 4.3 21.6 1.0 CA A:PRO232 4.3 14.1 1.0 N A:PHE234 4.3 15.3 1.0 C A:PRO233 4.5 16.2 1.0 C5' A:SAH401 4.5 14.6 1.0 CB A:ASN231 4.5 13.1 1.0 CE1 A:PHE234 4.6 16.3 1.0 CG A:SAH401 4.6 14.8 1.0 CA A:ASN231 4.7 13.7 1.0 CD1 A:PHE234 4.7 16.1 1.0 CD A:PRO232 4.9 14.8 1.0 CB A:PHE234 5.0 14.8 1.0

D.P.Cogan, A.Bhushan, R.Reyes, L.Zhu, J.Piel, S.K.Nair. Structure and Mechanism For Iterative Amide N -Methylation in the Biosynthesis of Channel-Forming Peptide Cytotoxins. Proc.Natl.Acad.Sci.Usa V. 119 78119 2022.
ISSN: ESSN 1091-6490
PubMed: 35316135
DOI: 10.1073/PNAS.2116578119