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Manganese in PDB 5v2x: Ethylene Forming Enzyme in Complex with Manganese and 2-Oxoglutarate

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

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

Protein crystallography data

The structure of Ethylene Forming Enzyme in Complex with Manganese and 2-Oxoglutarate, PDB code: 5v2x 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) 44.03 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.411, 97.546, 102.385, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Ethylene Forming Enzyme in Complex with Manganese and 2-Oxoglutarate (pdb code 5v2x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Ethylene Forming Enzyme in Complex with Manganese and 2-Oxoglutarate, PDB code: 5v2x:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 5v2x

Go back to Manganese Binding Sites List in 5v2x
Manganese binding site 1 out of 2 in the Ethylene Forming Enzyme 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 in Complex with Manganese and 2-Oxoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:13.3
occ:1.00
O2 A:AKG402 2.1 17.9 0.4
OD1 A:ASP191 2.2 12.8 1.0
NE2 A:HIS268 2.2 10.2 1.0
NE2 A:HIS189 2.2 15.4 1.0
O A:HOH531 2.3 17.6 1.0
O A:HOH508 2.3 14.4 1.0
O4 A:AKG403 2.4 18.1 0.5
CG A:ASP191 3.1 15.7 1.0
C1 A:AKG402 3.1 20.7 0.4
CE1 A:HIS268 3.1 11.5 1.0
CE1 A:HIS189 3.2 14.8 1.0
CD2 A:HIS268 3.2 13.3 1.0
OD2 A:ASP191 3.2 13.9 1.0
CD2 A:HIS189 3.2 12.8 1.0
C5 A:AKG403 3.3 20.9 0.5
O1 A:AKG402 3.5 19.1 0.4
O3 A:AKG403 3.7 19.0 0.5
O A:HOH582 4.0 21.3 1.0
ND1 A:HIS268 4.3 10.5 1.0
ND1 A:HIS189 4.3 12.3 1.0
C2 A:AKG402 4.3 20.7 0.4
CG A:HIS268 4.3 10.1 1.0
CG A:HIS189 4.4 9.7 1.0
O A:HOH540 4.4 32.9 1.0
CB A:ASP191 4.5 8.7 1.0
C4 A:AKG403 4.5 21.2 0.5
C3 A:AKG403 4.5 20.4 0.5
CA A:ASP191 4.9 11.5 1.0
C3 A:AKG402 4.9 20.5 0.4
CZ A:PHE283 4.9 22.3 1.0
O A:HOH875 4.9 27.2 1.0

Manganese binding site 2 out of 2 in 5v2x

Go back to Manganese Binding Sites List in 5v2x
Manganese binding site 2 out of 2 in the Ethylene Forming Enzyme 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 2 of Ethylene Forming Enzyme in Complex with Manganese and 2-Oxoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:13.4
occ:1.00
O2 B:AKG403 2.1 15.3 0.3
OD1 B:ASP191 2.1 11.5 1.0
NE2 B:HIS268 2.2 10.7 1.0
O B:HOH519 2.2 17.5 1.0
O B:HOH521 2.3 18.0 1.0
NE2 B:HIS189 2.3 14.5 1.0
O4 B:AKG402 2.3 15.6 0.5
C1 B:AKG403 2.9 19.9 0.3
CG B:ASP191 3.0 14.5 1.0
CE1 B:HIS268 3.1 12.8 1.0
C5 B:AKG402 3.2 20.6 0.5
CE1 B:HIS189 3.2 12.9 1.0
CD2 B:HIS268 3.2 11.9 1.0
CD2 B:HIS189 3.2 11.9 1.0
OD2 B:ASP191 3.3 13.2 1.0
O1 B:AKG403 3.3 19.7 0.3
O3 B:AKG402 3.5 19.5 0.5
O B:HOH625 4.1 20.8 1.0
C2 B:AKG403 4.1 19.0 0.3
ND1 B:HIS268 4.2 12.1 1.0
CG B:HIS268 4.3 9.5 1.0
ND1 B:HIS189 4.3 12.4 1.0
C4 B:AKG402 4.4 19.0 0.5
CG B:HIS189 4.4 14.6 1.0
C3 B:AKG402 4.4 21.0 0.5
C3 B:AKG403 4.4 20.9 0.3
CB B:ASP191 4.5 10.8 1.0
O B:HOH838 4.8 24.3 1.0
CA B:ASP191 4.8 11.6 1.0
N B:ASP191 5.0 10.5 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 03:08:16 2024

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