Atomistry » Manganese » PDB 6bh5-6dk4 » 6cba
Atomistry »
  Manganese »
    PDB 6bh5-6dk4 »
      6cba »

Manganese in PDB 6cba: Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Canavanine

Enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Canavanine

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

Protein crystallography data

The structure of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Canavanine, PDB code: 6cba 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) 32.49 / 1.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.430, 81.570, 87.630, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 16.3

Manganese Binding Sites:

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

Manganese binding site 1 out of 1 in 6cba

Go back to Manganese Binding Sites List in 6cba
Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and Canavanine


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 Canavanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:9.7
occ:1.00
O A:HOH501 2.0 50.2 1.0
O1 A:AKG402 2.1 12.3 0.9
NE2 A:HIS268 2.2 8.7 1.0
NE2 A:HIS189 2.2 10.2 1.0
O5 A:AKG402 2.3 15.7 0.9
OD1 A:ASP191 2.4 13.9 1.0
OD2 A:ASP191 2.4 13.8 1.0
CG A:ASP191 2.7 11.8 1.0
C1 A:AKG402 2.9 12.5 0.9
C2 A:AKG402 3.0 14.2 0.9
CE1 A:HIS268 3.1 8.7 1.0
CE1 A:HIS189 3.1 9.8 1.0
HNE A:GGB403 3.1 24.0 0.9
CD2 A:HIS268 3.2 8.4 1.0
CD2 A:HIS189 3.2 9.8 1.0
HE1 A:HIS189 3.3 11.7 1.0
HE1 A:HIS268 3.3 10.4 1.0
HD2 A:HIS268 3.4 10.1 1.0
HD2 A:HIS189 3.4 11.8 1.0
HN22 A:GGB403 3.6 25.6 0.9
HE1 A:PHE283 3.9 10.4 1.0
NE A:GGB403 4.0 20.0 0.9
HZ A:PHE283 4.0 10.4 1.0
O2 A:AKG402 4.1 14.3 0.9
CB A:ASP191 4.2 9.6 1.0
ND1 A:HIS268 4.3 8.2 1.0
ND1 A:HIS189 4.3 9.8 1.0
HZ A:PHE250 4.3 13.0 1.0
CG A:HIS268 4.3 8.0 1.0
CG A:HIS189 4.3 9.5 1.0
NH2 A:GGB403 4.4 21.4 0.9
HCG1 A:GGB403 4.4 20.4 0.9
C3 A:AKG402 4.5 14.7 0.9
O A:HOH822 4.5 34.0 1.0
CE1 A:PHE283 4.6 8.6 1.0
HB2 A:ASP191 4.6 11.5 1.0
HG11 A:VAL196 4.7 11.0 1.0
CZ A:PHE283 4.7 8.6 1.0
HB3 A:ASP191 4.7 11.5 1.0
CZ A:GGB403 4.7 21.9 0.9
HE2 A:PHE250 4.8 11.7 1.0
H42 A:AKG402 4.8 17.0 0.9
HA A:ASP191 4.8 10.4 1.0
H A:ASP191 4.8 10.1 1.0
H32 A:AKG402 4.8 17.6 0.9
N A:ASP191 4.8 8.4 1.0
CA A:ASP191 4.9 8.7 1.0
OD A:GGB403 5.0 19.1 0.9

Reference:

M.Fellner, M.Fellner, S.Martinez, J.Hu, R.P.Hausinger. N/A N/A.
Page generated: Tue Dec 15 04:51:19 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy