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Manganese in PDB 5vka: Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-L-Arginine

Enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-L-Arginine

All present enzymatic activity of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-L-Arginine:
1.13.12.19; 1.14.11.34;

Protein crystallography data

The structure of Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-L-Arginine, PDB code: 5vka 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) 38.70 / 1.17
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.583, 82.098, 87.766, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 18.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-L-Arginine (pdb code 5vka). 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 N-Omega-Hydroxy-L-Arginine, PDB code: 5vka:

Manganese binding site 1 out of 1 in 5vka

Go back to Manganese Binding Sites List in 5vka
Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Manganese, 2-Oxoglutarate and N-Omega-Hydroxy-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-Oxoglutarate and N-Omega-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:14.0
occ:1.00
 O A:HOH501 2.0 32.3 1.0
O1 A:AKG402 2.1 14.3 0.9
NE2 A:HIS268 2.2 9.9 1.0
NE2 A:HIS189 2.2 10.8 1.0
OD2 A:ASP191 2.2 13.8 1.0
O5 A:AKG402 2.4 14.9 0.9
OD1 A:ASP191 2.6 15.0 1.0
CG A:ASP191 2.7 12.1 1.0
C1 A:AKG402 2.9 14.8 0.9
C2 A:AKG402 3.1 15.1 0.9
CE1 A:HIS268 3.1 7.8 1.0
CE1 A:HIS189 3.1 10.9 1.0
CD2 A:HIS268 3.2 7.9 1.0
CD2 A:HIS189 3.2 9.6 1.0
HE1 A:HIS268 3.2 9.4 1.0
HE1 A:HIS189 3.2 13.1 1.0
HD2 A:HIS268 3.4 9.5 1.0
HD2 A:HIS189 3.4 11.5 1.0
HD3 A:HAR403 3.6 12.9 0.9
HD2 A:HAR403 3.9 12.9 0.9
HE1 A:PHE283 4.0 10.9 1.0
HZ A:PHE283 4.0 11.7 1.0
O2 A:AKG402 4.1 15.2 0.9
CD A:HAR403 4.2 10.8 0.9
ND1 A:HIS268 4.2 8.7 1.0
ND1 A:HIS189 4.2 11.2 1.0
CB A:ASP191 4.2 13.4 1.0
CG A:HIS189 4.3 10.3 1.0
CG A:HIS268 4.3 8.3 1.0
HZ A:PHE250 4.4 12.9 1.0
HB2 A:ASP191 4.5 16.1 1.0
HG2 A:HAR403 4.6 13.0 0.9
C3 A:AKG402 4.6 15.4 0.9
CE1 A:PHE283 4.6 9.1 1.0
CZ A:PHE283 4.7 9.7 1.0
HB3 A:ASP191 4.7 16.1 1.0
HG11 A:VAL196 4.7 11.2 1.0
NH2 A:HAR403 4.7 12.6 0.9
HE A:ARG171 4.8 12.9 1.0
HE2 A:PHE250 4.8 11.4 1.0
H A:ASP191 4.9 11.3 1.0
N A:ASP191 4.9 9.4 1.0
H42 A:AKG402 4.9 18.3 0.9
HA A:ASP191 4.9 13.8 1.0
H32 A:AKG402 4.9 18.5 0.9
CG A:HAR403 5.0 10.8 0.9
HD1 A:HIS268 5.0 10.4 1.0
HD1 A:HIS189 5.0 13.4 1.0
CA A:ASP191 5.0 11.5 1.0

Reference:

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
Page generated: Sun Oct 6 03:10:53 2024

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