Manganese in PDB 5v31: Ethylene Forming Enzyme in Complex with Manganese and L-Arginine

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

The structure of Ethylene Forming Enzyme in Complex with Manganese and L-Arginine, PDB code: 5v31 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)	43.58 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.630, 81.910, 87.160, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 24.7

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese and L-Arginine (pdb code 5v31). 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 L-Arginine, PDB code: 5v31:

Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese and L-Arginine


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 L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:25.8 occ:1.00 NE2 A:HIS189 2.1 19.2 1.0 OD2 A:ASP191 2.2 25.8 1.0 NE2 A:HIS268 2.3 23.8 1.0 O A:HOH620 2.6 21.7 1.0 OD1 A:ASP191 2.7 36.2 1.0 O A:HOH591 2.8 16.6 1.0 CG A:ASP191 2.8 30.7 1.0 CE1 A:HIS189 3.0 15.0 1.0 CD2 A:HIS268 3.1 23.8 1.0 CD2 A:HIS189 3.2 14.8 1.0 CE1 A:HIS268 3.3 22.6 1.0 ND1 A:HIS189 4.2 20.7 1.0 CG A:HIS189 4.3 20.1 1.0 CD A:ARG401 4.3 29.4 1.0 CG A:HIS268 4.3 23.9 1.0 CB A:ASP191 4.3 31.5 1.0 ND1 A:HIS268 4.4 26.2 1.0 CZ A:PHE283 4.6 22.4 1.0 CE1 A:PHE283 4.7 19.8 1.0 NH2 A:ARG401 4.9 38.0 1.0

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