Potassium in PDB 5icc: Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine

All present enzymatic activity of Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine:
2.1.1.128;

The structure of Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine, PDB code: 5icc was solved by A.Y.Robin, M.Graindorge, C.Giustini, R.Dumas, M.Matringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.81 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.640, 108.990, 40.910, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 20.6

The structure of Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Potassium atom in the Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine (pdb code 5icc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine, PDB code: 5icc:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:14.3 occ:0.50 O A:HOH626 3.0 6.4 1.0 NE2 A:HIS124 3.2 13.4 1.0 CE A:MET120 4.1 5.9 1.0 CD2 A:HIS124 4.1 8.2 1.0 CE1 A:HIS124 4.2 10.9 1.0 CB A:MET120 4.4 4.8 1.0 SD A:MET120 4.8 7.1 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of (S)-Norcoclaurine 6-O-Methyltransferase with S- Adenosyl-L-Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:K403 b:25.7 occ:1.00 CA A:HIS155 3.3 10.0 1.0 C A:HIS155 3.3 10.8 1.0 N A:GLU157 3.4 10.3 1.0 CB A:HIS155 3.4 10.1 1.0 N A:PRO156 3.5 11.3 1.0 O A:HOH581 3.5 17.0 1.0 CD A:PRO156 3.7 10.3 1.0 CB A:GLU157 3.8 13.0 1.0 O A:HIS155 3.9 11.0 1.0 N A:LYS158 4.0 8.8 1.0 CD2 A:HIS155 4.1 9.2 1.0 CG A:HIS155 4.1 8.0 1.0 CA A:GLU157 4.1 10.8 1.0 CG A:GLU157 4.2 22.4 1.0 C A:PRO156 4.3 10.4 1.0 CG A:PRO156 4.3 13.5 1.0 CG A:LYS158 4.4 11.5 1.0 CA A:PRO156 4.4 11.2 1.0 C A:GLU157 4.6 10.4 1.0 N A:HIS155 4.7 9.4 1.0 CB A:LYS158 4.9 8.8 1.0 O A:GLU154 5.0 9.6 1.0 CB A:PRO156 5.0 13.0 1.0

A.Y.Robin, C.Giustini, M.Graindorge, M.Matringe, R.Dumas. Crystal Structure of Norcoclaurine-6-O-Methyltransferase, A Key Rate-Limiting Step in the Synthesis of Benzylisoquinoline Alkaloids. Plant J. V. 87 641 2016.
ISSN: ESSN 1365-313X
PubMed: 27232113
DOI: 10.1111/TPJ.13225