Iron in PDB 8ghe: The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa

All present enzymatic activity of The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa:
1.13.11.31; 1.13.11.33;

The binding sites of Iron atom in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa (pdb code 8ghe). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa, PDB code: 8ghe:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:68.4 occ:1.00 NE2 B:HIS360 2.2 45.7 1.0 NE2 B:HIS365 2.2 49.2 1.0 O B:ILE663 2.3 74.4 1.0 NE2 B:HIS540 2.3 41.3 1.0 CE1 B:HIS365 3.0 49.1 1.0 CE1 B:HIS360 3.0 44.5 1.0 C B:ILE663 3.1 65.6 1.0 OD1 B:ASN544 3.1 54.5 1.0 OXT B:ILE663 3.1 67.8 1.0 CE1 B:HIS540 3.2 41.3 1.0 CD2 B:HIS540 3.3 27.2 1.0 CD2 B:HIS360 3.3 32.1 1.0 CD2 B:HIS365 3.4 42.8 1.0 CG B:ASN544 3.4 45.8 1.0 CB B:ASN544 3.8 36.9 1.0 ND1 B:HIS360 4.2 45.2 1.0 ND2 B:ASN544 4.2 45.6 1.0 ND1 B:HIS365 4.2 41.1 1.0 ND1 B:HIS540 4.3 41.1 1.0 CG B:HIS360 4.4 30.8 1.0 CG B:HIS540 4.4 37.7 1.0 CG B:HIS365 4.4 36.4 1.0 CA B:ILE663 4.5 56.3 1.0 N B:ILE663 4.8 58.3 1.0 CG1 B:VAL661 4.9 51.8 1.0 O B:LEU597 4.9 61.9 1.0

Iron binding site 2 out of 4 in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe701 b:68.4 occ:1.00 NE2 C:HIS360 2.2 45.7 1.0 NE2 C:HIS365 2.2 47.1 1.0 NE2 C:HIS540 2.3 39.2 1.0 O C:ILE663 2.3 75.2 1.0 CE1 C:HIS360 3.0 44.5 1.0 OD1 C:ASN544 3.0 54.4 1.0 CE1 C:HIS365 3.0 43.6 1.0 C C:ILE663 3.1 66.1 1.0 OXT C:ILE663 3.1 67.5 1.0 CE1 C:HIS540 3.2 42.2 1.0 CD2 C:HIS540 3.3 26.3 1.0 CD2 C:HIS360 3.3 32.1 1.0 CD2 C:HIS365 3.4 43.1 1.0 CG C:ASN544 3.5 45.7 1.0 CB C:ASN544 3.8 39.4 1.0 ND1 C:HIS360 4.2 45.2 1.0 ND1 C:HIS365 4.2 36.8 1.0 ND2 C:ASN544 4.3 48.8 1.0 ND1 C:HIS540 4.3 40.9 1.0 CG C:HIS360 4.4 30.8 1.0 CG C:HIS540 4.4 36.7 1.0 CG C:HIS365 4.4 33.3 1.0 CA C:ILE663 4.5 61.7 1.0 CG1 C:VAL661 4.8 48.5 1.0 N C:ILE663 4.9 61.3 1.0 O C:LEU597 4.9 61.8 1.0 CA C:ASN544 5.0 40.1 1.0

Iron binding site 3 out of 4 in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe701 b:68.4 occ:1.00 NE2 D:HIS360 2.2 45.7 1.0 NE2 D:HIS365 2.3 44.6 1.0 O D:ILE663 2.3 72.1 1.0 NE2 D:HIS540 2.3 38.4 1.0 CE1 D:HIS360 3.0 44.5 1.0 OD1 D:ASN544 3.0 54.0 1.0 CE1 D:HIS365 3.1 45.0 1.0 C D:ILE663 3.1 62.6 1.0 OXT D:ILE663 3.1 65.4 1.0 CE1 D:HIS540 3.2 40.7 1.0 CD2 D:HIS540 3.3 24.5 1.0 CD2 D:HIS360 3.3 32.1 1.0 CD2 D:HIS365 3.4 41.9 1.0 CG D:ASN544 3.4 46.6 1.0 CB D:ASN544 3.8 35.5 1.0 ND1 D:HIS360 4.2 45.2 1.0 ND2 D:ASN544 4.2 42.8 1.0 ND1 D:HIS365 4.3 39.0 1.0 ND1 D:HIS540 4.3 39.0 1.0 CG D:HIS360 4.4 30.8 1.0 CG D:HIS540 4.4 32.9 1.0 CG D:HIS365 4.4 38.6 1.0 CA D:ILE663 4.5 54.7 1.0 CG1 D:VAL661 4.8 49.2 1.0 N D:ILE663 4.9 54.5 1.0 O D:LEU597 4.9 63.8 1.0

Iron binding site 4 out of 4 in the The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Structure of H12-Lox in Tetrameric Form Bound to Endogenous Inhibitor Oleoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:68.4 occ:1.00 NE2 A:HIS360 2.2 45.7 1.0 NE2 A:HIS365 2.2 44.2 1.0 O A:ILE663 2.2 72.6 1.0 NE2 A:HIS540 2.2 39.3 1.0 CE1 A:HIS365 3.0 43.0 1.0 OD1 A:ASN544 3.0 52.1 1.0 CE1 A:HIS360 3.0 44.5 1.0 C A:ILE663 3.1 63.1 1.0 OXT A:ILE663 3.1 64.1 1.0 CE1 A:HIS540 3.2 42.5 1.0 CD2 A:HIS540 3.2 29.3 1.0 CD2 A:HIS360 3.3 32.1 1.0 CD2 A:HIS365 3.4 46.0 1.0 CG A:ASN544 3.5 45.7 1.0 C12 A:3VV702 3.9 53.9 1.0 CB A:ASN544 3.9 40.2 1.0 C13 A:3VV702 4.1 54.3 1.0 ND1 A:HIS365 4.2 34.9 1.0 ND1 A:HIS360 4.2 45.2 1.0 ND2 A:ASN544 4.3 48.4 1.0 ND1 A:HIS540 4.3 41.2 1.0 CG A:HIS540 4.4 35.6 1.0 CG A:HIS360 4.4 30.8 1.0 CG A:HIS365 4.4 36.7 1.0 CA A:ILE663 4.5 58.9 1.0 N A:ILE663 4.8 57.5 1.0 CG1 A:VAL661 4.9 49.7 1.0 C14 A:3VV702 5.0 44.4 1.0

J.I.Mobbs, K.A.Black, M.Tran, W.A.C.Burger, H.Venugopal, T.R.Holman, M.Holinstat, D.Thal, A.Glukhova. Cryo-Em Structures of Human Arachidonate 12S-Lipoxygenase (12-Lox) Bound to Endogenous and Exogenous Inhibitors. Blood 2023.
ISSN: ESSN 1528-0020
PubMed: 37506345
DOI: 10.1182/BLOOD.2023020441