Zinc in PDB 3bq6: Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ (Monoclinic)

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

The structure of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ (Monoclinic), PDB code: 3bq6 was solved by R.Pejchal, J.L.Smith, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.90 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.087, 107.604, 107.442, 90.00, 110.12, 90.00
R / Rfree (%)	21 / 23.8

The binding sites of Zinc atom in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ (Monoclinic) (pdb code 3bq6). 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+ (Monoclinic), PDB code: 3bq6:
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+ (Monoclinic)


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+ (Monoclinic) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn800 b:52.4 occ:1.00 NE2 A:HIS618 2.1 45.7 1.0 OE1 A:GLU642 2.1 34.8 1.0 SG A:CYS704 2.4 37.5 1.0 SG A:CYS620 2.4 40.0 1.0 CD2 A:HIS618 3.0 34.1 1.0 CE1 A:HIS618 3.1 32.1 1.0 CB A:CYS704 3.3 35.9 1.0 CD A:GLU642 3.4 42.7 1.0 CB A:CYS620 3.5 45.5 1.0 CA A:CYS620 3.8 32.9 1.0 O A:ASP703 4.0 33.7 1.0 CA A:CYS704 4.1 34.8 1.0 CG A:GLU642 4.1 32.8 1.0 CG A:HIS618 4.2 36.2 1.0 ND1 A:HIS618 4.2 33.0 1.0 OE2 A:GLU642 4.3 40.5 1.0 N A:CYS620 4.4 37.6 1.0 C A:MET619 4.8 32.7 1.0 C A:ASP703 4.8 34.0 1.0 O A:MET619 4.8 36.0 1.0 N A:CYS704 4.9 27.2 1.0

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


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+ (Monoclinic) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn801 b:61.7 occ:1.00 NE2 B:HIS618 2.1 47.8 1.0 OE1 B:GLU642 2.1 40.3 1.0 SG B:CYS704 2.4 35.4 1.0 SG B:CYS620 2.4 45.0 1.0 CD2 B:HIS618 3.0 35.4 1.0 CE1 B:HIS618 3.1 35.2 1.0 CB B:CYS704 3.2 36.5 1.0 CD B:GLU642 3.4 46.1 1.0 CB B:CYS620 3.5 43.9 1.0 CA B:CYS620 3.9 35.3 1.0 O B:ASP703 4.0 33.6 1.0 CA B:CYS704 4.0 36.8 1.0 CG B:GLU642 4.1 31.9 1.0 CG B:HIS618 4.2 35.7 1.0 ND1 B:HIS618 4.2 36.5 1.0 OE2 B:GLU642 4.3 45.4 1.0 N B:CYS620 4.5 38.9 1.0 C B:ASP703 4.8 34.0 1.0 O B:MET619 4.9 37.1 1.0 N B:CYS704 4.9 28.8 1.0 C B:MET619 4.9 34.9 1.0

M.Koutmos, R.Pejchal, T.M.Bomer, R.G.Matthews, J.L.Smith, M.L.Ludwig. Metal Active Site Elasticity Linked to Activation of Homocysteine in Methionine Synthases. Proc.Natl.Acad.Sci.Usa V. 105 3286 2008.
ISSN: ISSN 0027-8424
PubMed: 18296644
DOI: 10.1073/PNAS.0709960105