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

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

The structure of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Methyltetrahydrofolate, PDB code: 1xpg 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)	19.99 / 2.59
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	163.948, 159.303, 64.449, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 24.8

The binding sites of Zinc atom in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Methyltetrahydrofolate (pdb code 1xpg). 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 Methyltetrahydrofolate, PDB code: 1xpg:
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 Methyltetrahydrofolate


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 Methyltetrahydrofolate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1887 b:32.9 occ:1.00 NE2 A:HIS618 2.0 26.6 1.0 OE1 A:GLU642 2.1 30.3 1.0 SG A:CYS704 2.3 29.2 1.0 SG A:CYS620 2.3 33.0 1.0 CD2 A:HIS618 3.0 19.8 1.0 CE1 A:HIS618 3.1 21.0 1.0 CB A:CYS704 3.2 25.0 1.0 CB A:CYS620 3.3 28.0 1.0 CD A:GLU642 3.4 29.2 1.0 CA A:CYS620 3.6 28.4 1.0 O A:ASP703 3.9 23.7 1.0 CA A:CYS704 3.9 24.6 1.0 CG A:GLU642 4.1 25.5 1.0 N A:CYS620 4.2 29.2 1.0 ND1 A:HIS618 4.2 22.4 1.0 CG A:HIS618 4.2 21.9 1.0 OE2 A:GLU642 4.3 30.4 1.0 O A:HOH995 4.6 43.2 1.0 C A:ASP703 4.6 23.8 1.0 C A:MSE619 4.7 31.2 1.0 N A:CYS704 4.7 22.8 1.0 O A:MSE619 4.9 31.4 1.0 C A:CYS620 4.9 27.1 1.0

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


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 Methyltetrahydrofolate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1888 b:33.6 occ:1.00 NE2 B:HIS618 2.1 29.9 1.0 OE1 B:GLU642 2.1 31.8 1.0 SG B:CYS704 2.3 29.0 1.0 SG B:CYS620 2.3 31.6 1.0 CD2 B:HIS618 3.0 28.5 1.0 CB B:CYS704 3.0 25.4 1.0 CE1 B:HIS618 3.1 28.8 1.0 CB B:CYS620 3.3 28.9 1.0 CD B:GLU642 3.3 33.6 1.0 CA B:CYS620 3.7 28.7 1.0 CA B:CYS704 3.8 24.2 1.0 O B:ASP703 3.9 22.3 1.0 CG B:GLU642 4.0 30.4 1.0 CG B:HIS618 4.1 29.1 1.0 ND1 B:HIS618 4.2 29.3 1.0 N B:CYS620 4.2 30.1 1.0 OE2 B:GLU642 4.3 34.7 1.0 O B:HOH997 4.6 38.4 1.0 C B:ASP703 4.6 22.9 1.0 N B:CYS704 4.7 22.8 1.0 C B:MSE619 4.7 32.0 1.0 O B:MSE619 4.7 31.2 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