Chlorine in PDB 2ydy: Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form

The structure of Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form, PDB code: 2ydy was solved by W.W.Yue, N.Shafqat, J.R.C.Muniz, A.C.W.Pike, A.Chaikuad, C.K.Allerston, O.Gileadi, F.Von Delft, K.L.Kavanagh, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.07 / 2.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	40.980, 111.770, 123.120, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.8

The binding sites of Chlorine atom in the Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form (pdb code 2ydy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form, PDB code: 2ydy:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human S-Adenosylmethionine Synthetase 2, Beta Subunit in Orthorhombic Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1328 b:43.2 occ:0.50 N A:ALA287 3.9 36.8 1.0 CA A:GLY286 4.0 34.4 1.0 NH1 A:ARG289 4.1 48.8 1.0 NH2 A:ARG289 4.5 58.5 1.0 C A:GLY286 4.5 39.4 1.0 CB A:ALA287 4.6 36.8 1.0 CZ A:ARG289 4.8 66.5 1.0 CA A:ALA287 4.9 36.7 1.0

N.Shafqat, J.R.C.Muniz, E.S.Pilka, E.Papagrigoriou, F.Von Delft, U.Oppermann, W.W.Yue. Insight Into S-Adenosylmethionine Biosynthesis From the Crystal Structures of the Human Methionine Adenosyltransferase Catalytic and Regulatory Subunits. Biochem.J. V. 452 27 2013.
ISSN: ISSN 0264-6021
PubMed: 23425511
DOI: 10.1042/BJ20121580