Manganese in PDB 6cf3: Ethylene Forming Enzyme Y306A Variant in Complex with Manganese and 2- Oxoglutarate

All present enzymatic activity of Ethylene Forming Enzyme Y306A Variant in Complex with Manganese and 2- Oxoglutarate:
1.13.12.19; 1.14.11.34;

The structure of Ethylene Forming Enzyme Y306A Variant in Complex with Manganese and 2- Oxoglutarate, PDB code: 6cf3 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)	44.37 / 1.12
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.370, 85.410, 87.170, 90.00, 90.00, 90.00
R / Rfree (%)	14.8 / 16.7

The binding sites of Manganese atom in the Ethylene Forming Enzyme Y306A Variant in Complex with Manganese and 2- Oxoglutarate (pdb code 6cf3). 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 Y306A Variant in Complex with Manganese and 2- Oxoglutarate, PDB code: 6cf3:

Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme Y306A Variant in Complex with Manganese and 2- Oxoglutarate


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 Y306A Variant in Complex with Manganese and 2- Oxoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:7.8 occ:1.00 O2 A:AKG402 2.1 9.0 0.6 NE2 A:HIS268 2.2 7.1 1.0 NE2 A:HIS189 2.2 8.6 1.0 OD1 A:ASP191 2.3 11.6 1.0 O A:HOH503 2.3 29.1 1.0 O5 A:AKG402 2.3 11.3 0.6 O4 A:AKG402 2.3 18.7 0.4 O A:HOH501 2.3 12.5 0.4 OD2 A:ASP191 2.6 11.7 1.0 CG A:ASP191 2.8 9.8 1.0 C1 A:AKG402 2.9 9.1 0.6 C2 A:AKG402 3.0 9.8 0.6 CE1 A:HIS268 3.1 6.7 1.0 CE1 A:HIS189 3.2 8.7 1.0 CD2 A:HIS268 3.2 6.8 1.0 CD2 A:HIS189 3.2 7.5 1.0 HE1 A:HIS268 3.3 8.1 1.0 C5 A:AKG402 3.3 20.0 0.4 HE1 A:HIS189 3.3 10.4 1.0 HD2 A:HIS268 3.4 8.1 1.0 HD2 A:HIS189 3.4 9.1 1.0 HH21 A:ARG171 3.6 19.6 1.0 O3 A:AKG402 3.8 20.1 0.4 HE1 A:PHE283 4.0 12.2 1.0 O1 A:AKG402 4.1 10.4 0.6 C3 A:AKG402 4.2 20.6 0.4 O A:HOH502 4.2 37.2 1.0 ND1 A:HIS268 4.2 5.8 1.0 HZ A:PHE283 4.3 13.4 1.0 ND1 A:HIS189 4.3 7.7 1.0 CB A:ASP191 4.3 7.5 1.0 CG A:HIS268 4.3 6.3 1.0 CG A:HIS189 4.3 7.4 1.0 O A:HOH534 4.3 19.6 1.0 NH2 A:ARG171 4.4 16.3 1.0 C4 A:AKG402 4.4 20.6 0.4 HZ A:PHE250 4.5 11.5 1.0 C3 A:AKG402 4.5 10.9 0.6 HH22 A:ARG171 4.6 19.6 1.0 HB2 A:ASP191 4.7 9.0 1.0 H42 A:AKG402 4.7 13.7 0.6 CE1 A:PHE283 4.7 10.1 1.0 HB3 A:ASP191 4.8 9.0 1.0 HA A:ASP191 4.8 8.0 1.0 CZ A:PHE283 4.9 11.2 1.0 H32 A:AKG402 4.9 13.1 0.6 HG11 A:VAL196 4.9 9.4 1.0 HE A:ARG171 4.9 16.9 1.0 H31 A:AKG402 5.0 13.1 0.6 CA A:ASP191 5.0 6.7 1.0

M.Fellner, M.Fellner, S.Martinez, J.Hu, R.P.Hausinger. N/A N/A.