Manganese in PDB 5v2z: Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoadipic Acid and L-Arginine

All present enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoadipic Acid and L-Arginine:
1.13.12.19; 1.14.11.34;

The structure of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoadipic Acid and L-Arginine, PDB code: 5v2z 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)	41.69 / 1.23
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.450, 81.860, 87.570, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 16

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoadipic Acid and L-Arginine (pdb code 5v2z). 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, 2-Oxoadipic Acid and L-Arginine, PDB code: 5v2z:

Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoadipic Acid 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, 2-Oxoadipic Acid and L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:8.5 occ:1.00 O3 A:OOG402 2.1 11.6 1.0 OD2 A:ASP191 2.2 10.7 1.0 NE2 A:HIS189 2.2 8.5 1.0 NE2 A:HIS268 2.2 8.9 1.0 O5 A:OOG402 2.4 14.5 1.0 OD1 A:ASP191 2.6 11.4 1.0 CG A:ASP191 2.6 9.9 1.0 C6 A:OOG402 2.9 11.2 1.0 C5 A:OOG402 3.0 13.6 1.0 CE1 A:HIS268 3.1 8.1 1.0 CE1 A:HIS189 3.1 7.9 1.0 HE1 A:HIS268 3.2 9.7 1.0 CD2 A:HIS189 3.2 8.0 1.0 CD2 A:HIS268 3.2 8.8 1.0 HE1 A:HIS189 3.3 9.5 1.0 HD2 A:HIS189 3.4 9.7 1.0 HD2 A:HIS268 3.5 10.5 1.0 HD2 A:ARG403 3.6 12.2 1.0 HD3 A:ARG403 3.7 12.2 1.0 HH21 A:ARG403 3.9 12.2 1.0 HE1 A:PHE283 3.9 9.0 1.0 HZ A:PHE283 4.0 9.4 1.0 O4 A:OOG402 4.1 13.3 1.0 CD A:ARG403 4.1 10.2 1.0 CB A:ASP191 4.1 9.4 1.0 ND1 A:HIS268 4.2 8.2 1.0 ND1 A:HIS189 4.2 9.5 1.0 CG A:HIS189 4.3 8.6 1.0 CG A:HIS268 4.3 7.6 1.0 H32C A:OOG402 4.4 15.5 1.0 HZ A:PHE250 4.4 13.5 1.0 HB2 A:ASP191 4.4 11.3 1.0 HG3 A:ARG403 4.5 12.6 1.0 C4 A:OOG402 4.5 14.7 1.0 CE1 A:PHE283 4.6 7.5 1.0 HB3 A:ASP191 4.6 11.3 1.0 CZ A:PHE283 4.7 7.8 1.0 NH2 A:ARG403 4.7 10.2 1.0 HG11 A:VAL196 4.8 10.7 1.0 H A:ASP191 4.8 10.0 1.0 N A:ASP191 4.8 8.4 1.0 C3 A:OOG402 4.8 12.9 1.0 H31C A:OOG402 4.9 15.5 1.0 HE2 A:PHE250 4.9 10.3 1.0 CG A:ARG403 4.9 10.5 1.0 H41C A:OOG402 4.9 17.6 1.0 HA A:ASP191 4.9 9.6 1.0 CA A:ASP191 4.9 8.0 1.0 HE A:ARG171 5.0 11.7 1.0 HD1 A:HIS268 5.0 9.9 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