Manganese in PDB 5fno: Manganese Lipoxygenase

All present enzymatic activity of Manganese Lipoxygenase:
1.13.11.45;

The structure of Manganese Lipoxygenase, PDB code: 5fno was solved by A.Wennman, S.Karkehabadi, E.H.Oliw, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.705 / 2.04
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.725, 111.374, 171.224, 90.00, 90.00, 90.00
R / Rfree (%)	16.79 / 21.33

The binding sites of Manganese atom in the Manganese Lipoxygenase (pdb code 5fno). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Manganese Lipoxygenase, PDB code: 5fno:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Manganese Lipoxygenase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Manganese Lipoxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn606 b:33.0 occ:1.00 NE2 A:HIS469 2.1 27.9 1.0 OXT A:VAL605 2.1 37.4 1.0 NE2 A:HIS289 2.2 33.1 1.0 O A:HOH2173 2.3 35.1 1.0 NE2 A:HIS284 2.6 43.7 1.0 OD1 A:ASN473 2.9 34.4 1.0 CD2 A:HIS469 3.0 23.9 1.0 CD2 A:HIS284 3.1 42.7 1.0 C A:VAL605 3.1 38.2 1.0 CE1 A:HIS289 3.1 35.8 1.0 CD2 A:HIS289 3.1 31.6 1.0 CE1 A:HIS469 3.1 34.6 1.0 O A:VAL605 3.3 32.3 1.0 CG A:ASN473 3.7 36.7 1.0 CE1 A:HIS284 3.9 44.7 1.0 CB A:ASN473 4.0 30.4 1.0 CG A:HIS469 4.2 31.2 1.0 ND1 A:HIS469 4.2 30.4 1.0 ND1 A:HIS289 4.3 30.2 1.0 CG A:HIS289 4.3 26.3 1.0 CG A:HIS284 4.4 38.6 1.0 CA A:VAL605 4.5 37.8 1.0 CG1 A:VAL323 4.7 34.2 1.0 ND2 A:ASN473 4.7 33.0 1.0 N A:VAL605 4.7 30.2 1.0 CG1 A:VAL605 4.7 36.1 1.0 ND1 A:HIS284 4.7 41.2 1.0

Manganese binding site 2 out of 2 in the Manganese Lipoxygenase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Manganese Lipoxygenase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn606 b:33.1 occ:1.00 O B:VAL605 2.1 33.4 1.0 NE2 B:HIS469 2.2 36.4 1.0 O B:HOH2149 2.2 44.3 1.0 NE2 B:HIS289 2.2 34.4 1.0 NE2 B:HIS284 2.2 32.7 1.0 CD2 B:HIS469 2.9 30.9 1.0 OD1 B:ASN473 3.0 35.3 1.0 CD2 B:HIS284 3.1 31.3 1.0 C B:VAL605 3.2 42.1 1.0 CD2 B:HIS289 3.2 30.8 1.0 CE1 B:HIS289 3.2 34.1 1.0 CE1 B:HIS469 3.3 37.6 1.0 CE1 B:HIS284 3.3 35.5 1.0 OXT B:VAL605 3.5 36.6 1.0 CG B:ASN473 3.6 37.6 1.0 CB B:ASN473 3.9 30.7 1.0 CG B:HIS469 4.1 35.0 1.0 ND1 B:HIS469 4.3 32.8 1.0 CG B:HIS284 4.3 32.5 1.0 ND1 B:HIS289 4.3 37.9 1.0 CG B:HIS289 4.3 32.4 1.0 ND1 B:HIS284 4.4 38.1 1.0 CA B:VAL605 4.5 39.0 1.0 ND2 B:ASN473 4.5 38.1 1.0 CG2 B:VAL605 4.6 37.9 1.0 CG1 B:VAL323 4.6 43.6 1.0 O B:HOH2051 4.7 46.7 1.0 N B:VAL605 4.8 38.4 1.0

A.Wennman, E.H.Oliw, S.Karkehabadi, Y.Chen. Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe Oryzae J.Biol.Chem. V. 291 8130 2016.
ISSN: ISSN 0021-9258
PubMed: 26783260
DOI: 10.1074/JBC.M115.707380