Manganese in PDB 5vkb: Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Argininamide

All present enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Argininamide:
1.13.12.19; 1.14.11.34;

The structure of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Argininamide, PDB code: 5vkb 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)	38.68 / 1.14
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.482, 81.743, 87.811, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 16.4

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Argininamide (pdb code 5vkb). 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-Oxoglutarate and Argininamide, PDB code: 5vkb:

Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Argininamide


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-Oxoglutarate and Argininamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:11.2 occ:1.00 O1 A:AKG402 2.1 15.3 1.0 O A:HOH501 2.1 41.7 0.8 NE2 A:HIS268 2.2 9.9 1.0 NE2 A:HIS189 2.2 12.1 1.0 OD2 A:ASP191 2.3 14.9 1.0 O5 A:AKG402 2.4 18.2 1.0 OD1 A:ASP191 2.5 16.3 1.0 CG A:ASP191 2.7 14.3 1.0 C1 A:AKG402 2.9 16.1 1.0 C2 A:AKG402 3.0 16.3 1.0 CE1 A:HIS268 3.1 9.7 1.0 CE1 A:HIS189 3.1 11.8 1.0 CD2 A:HIS268 3.2 9.5 1.0 CD2 A:HIS189 3.2 10.8 1.0 HE1 A:HIS268 3.2 11.6 1.0 HE1 A:HIS189 3.3 14.1 1.0 HE A:AAR403 3.3 25.1 0.3 HD2 A:HIS189 3.4 13.0 1.0 HD2 A:HIS268 3.4 11.4 1.0 HD3 A:AAR403 3.6 18.0 0.5 HH11 A:AAR403 3.9 16.2 0.5 HD2 A:AAR403 3.9 18.0 0.5 HE1 A:PHE283 3.9 12.2 1.0 HH22 A:AAR403 4.0 27.5 0.3 HZ A:PHE283 4.0 13.0 1.0 O2 A:AKG402 4.1 17.8 1.0 NE A:AAR403 4.1 20.9 0.3 ND1 A:HIS268 4.2 9.0 1.0 CB A:ASP191 4.2 12.8 1.0 CD A:AAR403 4.2 15.0 0.5 HG2 A:AAR403 4.2 23.2 0.3 ND1 A:HIS189 4.2 11.8 1.0 CG A:HIS268 4.3 9.2 1.0 CG A:HIS189 4.3 11.4 1.0 HZ A:PHE250 4.3 15.0 1.0 C3 A:AKG402 4.5 17.5 1.0 HG2 A:AAR403 4.6 17.4 0.5 HB2 A:ASP191 4.6 15.3 1.0 CE1 A:PHE283 4.6 10.1 1.0 NH2 A:AAR403 4.7 22.9 0.3 CZ A:PHE283 4.7 10.8 1.0 HB3 A:ASP191 4.7 15.3 1.0 NH1 A:AAR403 4.7 13.5 0.5 HG11 A:VAL196 4.8 12.8 1.0 HE2 A:PHE250 4.8 12.8 1.0 H A:ASP191 4.9 12.1 1.0 N A:ASP191 4.9 10.1 1.0 H42 A:AKG402 4.9 20.3 1.0 HA A:ASP191 4.9 13.5 1.0 HE A:ARG171 4.9 14.8 1.0 H32 A:AKG402 4.9 21.1 1.0 CZ A:AAR403 4.9 22.3 0.3 CA A:ASP191 5.0 11.2 1.0 CG A:AAR403 5.0 14.5 0.5 HD1 A:HIS268 5.0 10.8 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