Zinc in PDB 3t0c: Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc

All present enzymatic activity of Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc:
2.1.1.14;

The structure of Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc, PDB code: 3t0c was solved by T.M.Fu, Y.H.Liang, X.D.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.07 / 2.19
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.845, 99.477, 77.883, 90.00, 94.55, 90.00
R / Rfree (%)	20.9 / 25.6

The binding sites of Zinc atom in the Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc (pdb code 3t0c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc, PDB code: 3t0c:

Zinc binding site 1 out of 1 in the Crystal Structure of Streptococcus Mutans Mete Complexed with Zinc


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 Streptococcus Mutans Mete Complexed with Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn749 b:39.7 occ:1.00 NE2 A:HIS630 2.0 36.0 1.0 SG A:CYS632 2.3 28.4 1.0 OE1 A:GLU654 2.5 45.0 1.0 SG A:CYS715 2.6 33.4 1.0 CD2 A:HIS630 3.0 36.9 1.0 CE1 A:HIS630 3.1 32.8 1.0 CB A:CYS632 3.3 29.8 1.0 CB A:CYS715 3.4 35.0 1.0 CD A:GLU654 3.5 49.5 1.0 CA A:CYS632 3.6 33.1 1.0 N A:CYS632 3.9 33.5 1.0 O A:HOH1061 3.9 34.2 1.0 OE2 A:GLU654 4.0 52.6 1.0 ND1 A:HIS630 4.1 32.1 1.0 CG A:HIS630 4.1 36.1 1.0 CA A:CYS715 4.3 39.4 1.0 O A:ASP714 4.3 39.5 1.0 CG A:GLU654 4.5 45.5 1.0 C A:MET631 4.6 36.9 1.0 O A:MET631 4.9 40.1 1.0

T.M.Fu, J.Almqvist, Y.H.Liang, L.Li, Y.Huang, X.D.Su. Crystal Structures of Cobalamin-Independent Methionine Synthase (Mete) From Streptococcus Mutans: A Dynamic Zinc-Inversion Model J.Mol.Biol. V. 412 688 2011.
ISSN: ISSN 0022-2836
PubMed: 21840320
DOI: 10.1016/J.JMB.2011.08.005