Sodium in PDB 5x62: Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy

All present enzymatic activity of Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy:
2.1.1.22;

The structure of Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy, PDB code: 5x62 was solved by W.Xie, X.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.44 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.537, 72.902, 175.235, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 24.3

The binding sites of Sodium atom in the Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy (pdb code 5x62). 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 Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy, PDB code: 5x62:

Sodium binding site 1 out of 1 in the Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of A Carnosine N-Methyltransferase Bound By Adohcy within 5.0Å range: probe atom residue distance (Å) B Occ B:Na502 b:39.3 occ:1.00 O B:HOH704 2.2 46.5 1.0 O B:HOH700 2.2 48.5 1.0 O B:LEU294 2.2 36.4 1.0 OD1 B:ASN266 2.3 36.1 1.0 O B:HIS292 2.4 38.4 1.0 O B:GLY291 2.4 35.9 1.0 C B:HIS292 3.1 38.2 1.0 C B:LEU294 3.4 39.9 1.0 CG B:ASN266 3.5 41.1 1.0 C B:GLY291 3.5 40.5 1.0 CA B:HIS292 3.6 35.9 1.0 N B:LEU294 3.8 32.6 1.0 N B:ASN266 4.0 38.3 1.0 N B:HIS292 4.0 32.6 1.0 N B:VAL293 4.1 37.0 1.0 CA B:ASN266 4.2 38.9 1.0 CA B:LEU294 4.2 36.5 1.0 C B:VAL293 4.3 36.5 1.0 ND2 B:ASN266 4.4 44.5 1.0 CB B:ASN266 4.4 39.3 1.0 N B:LYS295 4.4 37.9 1.0 CA B:VAL293 4.7 35.2 1.0 CA B:LYS295 4.7 41.5 1.0 CB B:LEU294 4.8 37.3 1.0 CA B:GLY291 4.8 36.6 1.0 O B:VAL293 4.9 35.9 1.0 CG B:GLU265 4.9 43.7 1.0 C B:LYS295 4.9 38.5 1.0

X.Liu, J.Wu, Y.Sun, W.Xie. Substrate Recognition Mechanism of the Putative Yeast Carnosine N-Methyltransferase Acs Chem. Biol. V. 12 2164 2017.
ISSN: ESSN 1554-8937
PubMed: 28654751
DOI: 10.1021/ACSCHEMBIO.7B00328