Zinc in PDB 4rvg: Crystal Structure of Mtmc in Complex with Sam and Tdp

The structure of Crystal Structure of Mtmc in Complex with Sam and Tdp, PDB code: 4rvg was solved by O.V.Tsodikov, C.Hou, J.-M.Chen, J.Rohr, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.30
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	134.733, 134.733, 127.755, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 23.8

The binding sites of Zinc atom in the Crystal Structure of Mtmc in Complex with Sam and Tdp (pdb code 4rvg). 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 Mtmc in Complex with Sam and Tdp, PDB code: 4rvg:

Zinc binding site 1 out of 1 in the Crystal Structure of Mtmc in Complex with Sam and Tdp


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 Mtmc in Complex with Sam and Tdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:57.9 occ:1.00 SG A:CYS13 2.3 52.6 1.0 SG A:CYS59 2.3 55.1 1.0 SG A:CYS56 2.3 58.5 1.0 SG A:CYS16 2.3 56.7 1.0 CB A:CYS13 3.3 54.8 1.0 CB A:CYS56 3.4 58.1 1.0 CB A:CYS16 3.4 56.2 1.0 CB A:CYS59 3.4 56.3 1.0 N A:CYS59 3.7 57.0 1.0 N A:CYS16 3.8 54.1 1.0 CA A:CYS59 4.1 56.1 1.0 CA A:CYS16 4.2 55.8 1.0 CB A:SER58 4.4 55.3 1.0 CB A:LEU61 4.6 49.7 1.0 N A:ARG60 4.6 55.3 1.0 N A:GLY17 4.7 59.3 1.0 C A:CYS59 4.7 55.5 1.0 C A:CYS16 4.7 57.8 1.0 CA A:CYS13 4.8 54.3 1.0 CB A:MET15 4.8 51.5 1.0 CA A:CYS56 4.8 56.9 1.0 OG A:SER58 4.8 55.3 1.0 N A:LEU61 4.8 51.9 1.0 C A:SER58 4.8 57.2 1.0 N A:ALA18 4.9 63.0 1.0 CB A:ALA18 5.0 63.1 1.0 C A:MET15 5.0 51.7 1.0 O A:CYS56 5.0 57.8 1.0

J.M.Chen, C.Hou, G.Wang, O.V.Tsodikov, J.Rohr. Structural Insight Into Mtmc, A Bifunctional Ketoreductase-Methyltransferase Involved in the Assembly of the Mithramycin Trisaccharide Chain. Biochemistry 2015.
ISSN: ISSN 0006-2960
PubMed: 25587924
DOI: 10.1021/BI501462G