Iron in PDB 3d3l: The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target)

All present enzymatic activity of The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target):
1.13.11.31;

The structure of The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target), PDB code: 3d3l was solved by L.Tresaugues, M.Moche, C.H.Arrowsmith, H.Berglund, R.D.Busam, R.Collins, L.G.Dahlgren, A.M.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, M.D.Herman, A.Johansson, I.Johansson, A.Kallas, T.Karlberg, T.Kotenyova, L.Lehtio, M.E.Nilsson, T.Nyman, K.Olesen, C.Persson, J.Sagemark, H.Schueler, L.Svensson, A.G.Thorsell, S.Van Den Berg, M.Welin, J.Weigelt, M.Wikstrom, P.Nordlund, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.19 / 2.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	59.590, 70.153, 77.868, 65.37, 88.01, 69.82
R / Rfree (%)	20.6 / 27.6

The binding sites of Iron atom in the The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target) (pdb code 3d3l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target), PDB code: 3d3l:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:13.7 occ:1.00 NE2 A:HIS365 1.9 18.9 1.0 NE2 A:HIS540 1.9 18.5 1.0 NE2 A:HIS360 2.0 12.0 1.0 O A:HOH802 2.1 2.0 1.0 CE1 A:HIS365 2.7 19.5 1.0 CD2 A:HIS540 2.9 19.4 1.0 CE1 A:HIS360 2.9 12.4 1.0 CD2 A:HIS365 2.9 19.5 1.0 CE1 A:HIS540 3.0 18.9 1.0 CD2 A:HIS360 3.0 13.2 1.0 ND2 A:ASN544 3.6 16.9 1.0 ND1 A:HIS365 3.8 19.8 1.0 CG A:ASN544 3.9 19.9 1.0 CG A:HIS365 4.0 19.7 1.0 ND1 A:HIS360 4.0 13.3 1.0 CG A:HIS540 4.0 18.2 1.0 ND1 A:HIS540 4.0 18.3 1.0 CG A:HIS360 4.1 14.2 1.0 CB A:ASN544 4.4 20.7 1.0 OD1 A:ASN544 4.4 18.8 1.0

Iron binding site 2 out of 2 in the The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The 2.6 A Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type (Casp Target) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:14.8 occ:1.00 NE2 B:HIS365 1.9 18.9 1.0 NE2 B:HIS360 2.0 16.9 1.0 O B:HOH802 2.1 2.0 1.0 NE2 B:HIS540 2.1 18.8 1.0 CE1 B:HIS365 2.6 19.1 1.0 CD2 B:HIS540 2.9 18.9 1.0 CE1 B:HIS360 2.9 17.5 1.0 CD2 B:HIS360 2.9 17.1 1.0 CD2 B:HIS365 3.1 18.0 1.0 CE1 B:HIS540 3.2 19.1 1.0 ND2 B:ASN544 3.7 21.0 1.0 ND1 B:HIS365 3.8 18.4 1.0 CG B:ASN544 4.0 21.5 1.0 ND1 B:HIS360 4.0 16.3 1.0 CG B:HIS360 4.1 16.7 1.0 CG B:HIS365 4.1 17.9 1.0 CG B:HIS540 4.1 18.0 1.0 ND1 B:HIS540 4.2 19.5 1.0 CB B:ASN544 4.4 21.6 1.0 OD1 B:ASN544 4.5 20.1 1.0 CG2 B:THR364 4.8 18.4 1.0

L.Tresaugues, M.Moche, C.H.Arrowsmith, H.Berglund, R.D.Busam, R.Collins, L.G.Dahlgren, A.M.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, M.D.Herman, A.Johansson, I.Johansson, A.Kallas, T.Karlberg, T.Kotenyova, L.Lehtio, M.E.Nilsson, T.Nyman, K.Olesen, C.Persson, J.Sagemark, H.Schueler, L.Svensson, A.G.Thorsell, S.Van Den Berg, M.Welin, J.Weigelt, M.Wikstrom, P.Nordlund. Crystal Structure of the Lipoxygenase Domain of Human Arachidonate 12-Lipoxygenase, 12S-Type. To Be Published.