Sodium in PDB 7kb1: Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate

The structure of Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate, PDB code: 7kb1 was solved by J.L.Brewster, P.Pachl, C.Squire, M.Selmer, W.M.Patrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.37 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.58, 151.34, 91.39, 90, 112.04, 90
R / Rfree (%)	22.7 / 26.2

The structure of Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Sodium atom in the Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate (pdb code 7kb1). 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 Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate, PDB code: 7kb1:

Sodium binding site 1 out of 1 in the Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:68.7 occ:1.00 O A:HOH772 2.7 52.7 1.0 O A:HOH805 3.2 33.3 0.5 OE2 A:GLU52 3.4 62.8 1.0 OE1 A:GLU52 3.4 62.0 1.0 CD A:GLU52 3.8 61.4 1.0

J.L.Brewster, P.Pachl, J.L.O.Mckellar, M.Selmer, C.J.Squire, W.M.Patrick. Structures and Kinetics of Thermotoga Maritima Mety Reveal New Insights Into the Predominant Sulfurylation Enzyme of Bacterial Methionine Biosynthesis. J.Biol.Chem. 00797 2021.
ISSN: ESSN 1083-351X
PubMed: 34019879
DOI: 10.1016/J.JBC.2021.100797