Zinc in PDB 3bq5: Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine (Monoclinic)

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

The structure of Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine (Monoclinic), PDB code: 3bq5 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)	47.40 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.229, 107.164, 107.667, 90.00, 108.96, 90.00
R / Rfree (%)	21.7 / 24

The binding sites of Zinc atom in the Crystal Structure of T. Maritima Cobalamin-Independent Methionine Synthase Complexed with ZN2+ and Homocysteine (Monoclinic) (pdb code 3bq5). 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 (Monoclinic), PDB code: 3bq5:
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 (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+ and Homocysteine (Monoclinic) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn800 b:26.9 occ:1.00 NE2 A:HIS618 2.1 27.0 1.0 SG A:CYS620 2.3 27.9 1.0 SG A:CYS704 2.3 29.6 1.0 SD A:HCS802 2.4 27.3 1.0 CD2 A:HIS618 3.0 24.4 1.0 CE1 A:HIS618 3.2 26.4 1.0 CB A:CYS620 3.2 31.3 1.0 CG A:HCS802 3.3 27.0 1.0 CB A:CYS704 3.5 28.1 1.0 CB A:HCS802 4.0 28.6 1.0 CG A:HIS618 4.2 30.5 1.0 CA A:CYS704 4.2 27.9 1.0 ND1 A:HIS618 4.2 25.4 1.0 CA A:CYS620 4.5 27.7 1.0 N A:CYS620 4.6 32.8 1.0 N A:GLY705 4.7 30.0 1.0 O A:ASP703 4.8 27.6 1.0 CG2 A:ILE409 4.8 24.9 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 (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+ and Homocysteine (Monoclinic) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn801 b:28.4 occ:1.00 NE2 B:HIS618 2.0 26.7 1.0 SD B:HCS803 2.3 27.6 1.0 SG B:CYS704 2.3 28.1 1.0 SG B:CYS620 2.4 29.4 1.0 CD2 B:HIS618 2.9 27.0 1.0 CE1 B:HIS618 3.1 29.5 1.0 CG B:HCS803 3.2 27.0 1.0 CB B:CYS620 3.2 31.0 1.0 CB B:CYS704 3.6 25.9 1.0 CB B:HCS803 3.9 34.0 1.0 CG B:HIS618 4.1 32.6 1.0 ND1 B:HIS618 4.1 27.5 1.0 O B:HOH894 4.2 43.2 1.0 CA B:CYS704 4.2 24.6 1.0 CA B:CYS620 4.5 29.1 1.0 N B:CYS620 4.6 29.7 1.0 N B:GLY705 4.7 29.0 1.0 CG2 B:ILE409 4.7 24.5 1.0 O B:ASP703 4.8 31.8 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