Manganese in PDB 5v2t: Ethylene Forming Enzyme in Complex with Manganese and Tartrate

All present enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese and Tartrate:
1.13.12.19; 1.14.11.34;

The structure of Ethylene Forming Enzyme in Complex with Manganese and Tartrate, PDB code: 5v2t was solved by M.Fellner, S.Martinez, J.Hu, R.P.Hausinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.99 / 1.23
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	79.832, 97.785, 97.982, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 15.3

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese and Tartrate (pdb code 5v2t). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Ethylene Forming Enzyme in Complex with Manganese and Tartrate, PDB code: 5v2t:

Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese and Tartrate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ethylene Forming Enzyme in Complex with Manganese and Tartrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:10.2 occ:1.00 OD1 A:ASP191 2.2 10.8 1.0 O41 A:TLA402 2.2 12.9 1.0 O A:HOH641 2.2 14.9 1.0 NE2 A:HIS268 2.2 9.5 1.0 O A:HOH524 2.2 12.3 1.0 NE2 A:HIS189 2.3 10.3 1.0 CG A:ASP191 3.1 10.1 1.0 CE1 A:HIS189 3.1 10.3 1.0 C4 A:TLA402 3.2 15.0 1.0 CE1 A:HIS268 3.2 9.1 1.0 CD2 A:HIS268 3.2 8.9 1.0 HE1 A:HIS189 3.3 12.4 1.0 OD2 A:ASP191 3.3 11.3 1.0 CD2 A:HIS189 3.3 9.6 1.0 HE1 A:HIS268 3.3 10.9 1.0 HD2 A:HIS268 3.4 10.6 1.0 O4 A:TLA402 3.5 15.4 1.0 HD2 A:HIS189 3.5 11.5 1.0 HZ A:PHE283 4.0 20.5 0.6 O2 A:TLA402 4.1 20.9 1.0 O A:HOH667 4.2 22.5 1.0 HA A:TLA402 4.2 25.0 1.0 HZ A:PHE283 4.2 17.6 0.4 ND1 A:HIS189 4.3 10.1 1.0 ND1 A:HIS268 4.3 8.5 1.0 CG A:HIS268 4.3 8.3 1.0 CG A:HIS189 4.4 9.2 1.0 H2 A:TLA402 4.4 22.5 1.0 C3 A:TLA402 4.4 16.6 1.0 CB A:ASP191 4.5 10.0 1.0 HA A:ASP191 4.5 11.5 1.0 HZ A:PHE250 4.5 14.5 1.0 C2 A:TLA402 4.6 18.8 1.0 HE1 A:PHE283 4.7 17.9 0.4 O A:HOH878 4.8 24.7 1.0 HE A:ARG171 4.8 17.1 1.0 CZ A:PHE283 4.8 17.1 0.6 H3 A:TLA402 4.8 19.9 1.0 HE2 A:PHE283 4.9 16.8 0.6 CA A:ASP191 4.9 9.6 1.0 HB3 A:ASP191 5.0 12.0 1.0 CZ A:PHE283 5.0 14.7 0.4

S.Martinez, M.Fellner, C.Q.Herr, A.Ritchie, J.Hu, R.P.Hausinger. Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates A Twist. J. Am. Chem. Soc. V. 139 11980 2017.
ISSN: ESSN 1520-5126
PubMed: 28780854
DOI: 10.1021/JACS.7B06186