Zinc in PDB 1xdj: Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine

All present enzymatic activity of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine:
2.1.1.14;

The structure of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine, PDB code: 1xdj was solved by R.Pejchal, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	167.053, 159.366, 65.639, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 26.8

The binding sites of Zinc atom in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine (pdb code 1xdj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine, PDB code: 1xdj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1051 b:27.8 occ:1.00 NE2 A:HIS618 2.1 21.7 1.0 SG A:CYS620 2.2 27.0 1.0 SG A:CYS704 2.2 23.3 1.0 CE1 A:HIS618 2.9 15.4 1.0 OE1 A:GLU642 2.9 31.0 1.0 SD A:HCS1049 3.1 25.0 1.0 CD2 A:HIS618 3.2 17.6 1.0 CB A:CYS704 3.2 16.4 1.0 CB A:CYS620 3.5 28.8 1.0 CA A:CYS704 4.0 15.5 1.0 ND1 A:HIS618 4.0 16.7 1.0 CA A:CYS620 4.0 28.1 1.0 CD A:GLU642 4.1 31.3 1.0 CG A:HIS618 4.2 17.0 1.0 N A:CYS620 4.3 27.8 1.0 O A:ASP703 4.3 11.4 1.0 CG A:HCS1049 4.4 21.7 1.0 C A:MSE619 4.6 28.4 1.0 CG A:GLU642 4.6 27.8 1.0 O A:MSE619 4.8 28.2 1.0 N A:GLY705 4.9 14.6 1.0 CG2 A:ILE409 4.9 11.9 1.0 N A:CYS704 5.0 15.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1052 b:30.8 occ:1.00 NE2 B:HIS618 2.1 25.2 1.0 SG B:CYS620 2.2 25.4 1.0 SG B:CYS704 2.2 25.2 1.0 OE1 B:GLU642 2.9 29.6 1.0 CD2 B:HIS618 3.0 20.9 1.0 CE1 B:HIS618 3.1 20.8 1.0 SD A:HCS1050 3.1 29.0 1.0 CB B:CYS704 3.3 16.9 1.0 CB B:CYS620 3.5 27.8 1.0 CA B:CYS620 4.0 28.0 1.0 CA B:CYS704 4.0 17.1 1.0 CD B:GLU642 4.1 29.0 1.0 CG B:HIS618 4.1 21.3 1.0 ND1 B:HIS618 4.2 21.3 1.0 O B:ASP703 4.3 13.3 1.0 CG A:HCS1050 4.3 24.4 1.0 N B:CYS620 4.4 26.3 1.0 C B:MSE619 4.7 26.8 1.0 CG B:GLU642 4.8 26.5 1.0 O B:MSE619 4.8 25.6 1.0 N B:GLY705 4.9 16.3 1.0 CG2 B:ILE409 4.9 11.3 1.0 N B:CYS704 4.9 15.6 1.0 CB A:HCS1050 5.0 21.7 1.0 C B:ASP703 5.0 14.7 1.0

R.Pejchal, M.L.Ludwig. Cobalamin-Independent Methionine Synthase (Mete): A Face-to-Face Double Barrel That Evolved By Gene Duplication Plos Biol. V. 3 E31 2005.
ISSN: ISSN 1544-9173
PubMed: 15630480
DOI: 10.1371/JOURNAL.PBIO.0030031