Calcium in PDB 2idj: Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form

All present enzymatic activity of Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form:
2.1.1.20;

The structure of Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form, PDB code: 2idj was solved by Z.Luka, S.Pakhomova, L.V.Loukachevitch, M.Egli, M.E.Newcomer, C.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.11 / 2.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.869, 85.223, 131.861, 90.00, 91.40, 90.00
R / Rfree (%)	22.2 / 27.2

The binding sites of Calcium atom in the Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form (pdb code 2idj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form, PDB code: 2idj:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca293 b:40.9 occ:1.00 OD1 B:ASN211 2.3 29.0 1.0 O B:HOH297 2.8 17.1 1.0 CG B:ASN211 3.3 23.3 1.0 ND2 B:ASN211 3.7 25.1 1.0 O D:SER182 4.3 20.5 1.0 O B:ASN211 4.6 21.4 1.0 CB B:ASN211 4.7 15.9 1.0 O B:HOH329 4.8 21.4 1.0 CA B:ASN211 4.9 17.9 1.0 C D:SER182 4.9 21.5 1.0 O D:LEU181 4.9 36.4 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca293 b:54.0 occ:1.00 OE2 C:GLU15 2.7 46.5 1.0 OE1 C:GLU15 3.0 29.8 1.0 CD C:GLU15 3.0 48.6 1.0 O D:HOH320 3.1 36.4 1.0 CG C:GLU15 4.2 51.7 1.0 CE1 D:HIS142 4.4 18.3 1.0 O D:GLY137 4.5 32.0 1.0 NE2 D:HIS142 4.8 20.4 1.0 CE D:MET90 4.9 26.6 1.0 OG D:SER139 4.9 47.6 1.0

Z.Luka, S.Pakhomova, L.V.Loukachevitch, M.Egli, M.E.Newcomer, C.Wagner. 5-Methyltetrahydrofolate Is Bound in Intersubunit Areas of Rat Liver Folate-Binding Protein Glycine N-Methyltransferase. J.Biol.Chem. V. 282 4069 2007.
ISSN: ISSN 0021-9258
PubMed: 17158459
DOI: 10.1074/JBC.M610384200