Zinc in PDB 1u22: A. Thaliana Cobalamine Independent Methionine Synthase

All present enzymatic activity of A. Thaliana Cobalamine Independent Methionine Synthase:
2.1.1.14;

The structure of A. Thaliana Cobalamine Independent Methionine Synthase, PDB code: 1u22 was solved by J.-L.Ferrer, S.Ravanel, M.Robert, R.Dumas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.78 / 2.65
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	122.423, 122.423, 131.365, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 27

The binding sites of Zinc atom in the A. Thaliana Cobalamine Independent Methionine Synthase (pdb code 1u22). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A. Thaliana Cobalamine Independent Methionine Synthase, PDB code: 1u22:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the A. Thaliana Cobalamine Independent Methionine Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A. Thaliana Cobalamine Independent Methionine Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn766 b:62.4 occ:1.00 O A:HOH774 2.5 42.7 1.0 SG A:CYS649 2.5 58.1 1.0 SG A:CYS733 2.7 57.6 1.0 NE2 A:HIS647 2.8 61.9 1.0 CB A:CYS733 3.2 60.5 1.0 CD2 A:HIS647 3.4 60.5 1.0 CB A:CYS649 3.4 59.5 1.0 CA A:CYS649 3.8 59.6 1.0 CE1 A:HIS647 3.9 60.6 1.0 CA A:CYS733 4.0 61.0 1.0 CG A:HCS772 4.0 45.8 1.0 O A:ASP732 4.1 66.7 1.0 N A:CYS649 4.2 59.2 1.0 SD A:HCS772 4.2 47.1 1.0 C A:MSE648 4.5 58.7 1.0 CG A:HIS647 4.6 59.5 1.0 O A:MSE648 4.6 60.7 1.0 ND1 A:HIS647 4.8 59.8 1.0 C A:ASP732 4.9 66.8 1.0 N A:CYS733 4.9 63.6 1.0 CG2 A:ILE437 4.9 62.5 1.0

Zinc binding site 2 out of 2 in the A. Thaliana Cobalamine Independent Methionine Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A. Thaliana Cobalamine Independent Methionine Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn767 b:41.8 occ:1.00 NE2 A:HIS658 2.1 42.4 1.0 OD2 A:ASP662 2.1 48.5 1.0 CE1 A:HIS658 2.9 42.0 1.0 CG A:ASP662 3.1 48.8 1.0 CD2 A:HIS658 3.1 43.5 1.0 OD1 A:ASP662 3.4 50.7 1.0 ND1 A:HIS658 4.0 42.1 1.0 CG A:HIS658 4.1 43.6 1.0 CB A:ASP662 4.3 48.7 1.0

J.-L.Ferrer, S.Ravanel, M.Robert, R.Dumas. Crystal Structures of Cobalamin-Independent Methionine Synthase Complexed with Zinc, Homocysteine, and Methyltetrahydrofolate J.Biol.Chem. V. 279 44235 2004.
ISSN: ISSN 0021-9258
PubMed: 15326182
DOI: 10.1074/JBC.C400325200