Iron in PDB 3bne: Lipoxygenase-1 (Soybean) I553A Mutant

All present enzymatic activity of Lipoxygenase-1 (Soybean) I553A Mutant:
1.13.11.12;

The structure of Lipoxygenase-1 (Soybean) I553A Mutant, PDB code: 3bne was solved by D.R.Tomchick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.72 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	94.115, 92.951, 49.416, 90.00, 90.76, 90.00
R / Rfree (%)	16.6 / 18.6

The binding sites of Iron atom in the Lipoxygenase-1 (Soybean) I553A Mutant (pdb code 3bne). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Lipoxygenase-1 (Soybean) I553A Mutant, PDB code: 3bne:

Iron binding site 1 out of 1 in the Lipoxygenase-1 (Soybean) I553A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Lipoxygenase-1 (Soybean) I553A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe840 b:19.2 occ:0.90 O A:HOH841 2.2 23.8 1.0 NE2 A:HIS690 2.2 12.6 1.0 NE2 A:HIS499 2.2 22.1 1.0 OXT A:ILE839 2.2 22.9 1.0 NE2 A:HIS504 2.3 21.2 1.0 OD1 A:ASN694 2.4 17.7 1.0 CE1 A:HIS499 3.0 23.8 1.0 CE1 A:HIS690 3.1 13.1 1.0 CE1 A:HIS504 3.2 20.8 1.0 C A:ILE839 3.2 23.8 1.0 CD2 A:HIS690 3.2 12.6 1.0 CD2 A:HIS499 3.3 21.7 1.0 CD2 A:HIS504 3.4 20.3 1.0 CG A:ASN694 3.4 15.7 1.0 O A:ILE839 3.5 24.4 1.0 CB A:ASN694 4.0 13.9 1.0 ND1 A:HIS499 4.2 24.3 1.0 ND1 A:HIS690 4.3 13.3 1.0 O A:HOH1158 4.3 50.4 1.0 CG A:HIS690 4.3 12.5 1.0 ND1 A:HIS504 4.4 20.2 1.0 CG A:HIS499 4.4 20.4 1.0 ND2 A:ASN694 4.4 14.0 1.0 CG A:HIS504 4.5 19.2 1.0 CG2 A:ILE837 4.6 20.9 1.0 CA A:ILE839 4.6 21.6 1.0 N A:ILE839 4.8 20.6 1.0 CG2 A:ILE839 4.9 24.2 1.0

M.P.Meyer, D.R.Tomchick, J.P.Klinman. Enzyme Structure and Dynamics Affect Hydrogen Tunneling: the Impact of A Remote Side Chain (I553) in Soybean Lipoxygenase-1. Proc.Natl.Acad.Sci.Usa V. 105 1146 2008.
ISSN: ISSN 0027-8424
PubMed: 18216254
DOI: 10.1073/PNAS.0710643105