Iron in PDB 3bnd: Lipoxygenase-1 (Soybean), I553V Mutant

All present enzymatic activity of Lipoxygenase-1 (Soybean), I553V Mutant:
1.13.11.12;

The structure of Lipoxygenase-1 (Soybean), I553V Mutant, PDB code: 3bnd 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)	27.37 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	94.012, 93.004, 49.351, 90.00, 90.61, 90.00
R / Rfree (%)	16.8 / 20

The binding sites of Iron atom in the Lipoxygenase-1 (Soybean), I553V Mutant (pdb code 3bnd). 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), I553V Mutant, PDB code: 3bnd:

Iron binding site 1 out of 1 in the Lipoxygenase-1 (Soybean), I553V 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), I553V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe840 b:24.1 occ:0.90 O A:HOH841 2.1 25.6 1.0 NE2 A:HIS499 2.2 23.1 1.0 NE2 A:HIS690 2.2 18.0 1.0 OXT A:ILE839 2.2 22.5 1.0 NE2 A:HIS504 2.3 25.0 1.0 OD1 A:ASN694 2.5 25.4 1.0 CE1 A:HIS499 3.0 26.4 1.0 CE1 A:HIS690 3.1 19.8 1.0 CE1 A:HIS504 3.2 22.8 1.0 C A:ILE839 3.2 24.3 1.0 CD2 A:HIS690 3.2 18.5 1.0 CD2 A:HIS499 3.3 22.8 1.0 CD2 A:HIS504 3.4 22.7 1.0 CG A:ASN694 3.4 21.7 1.0 O A:ILE839 3.5 24.5 1.0 CB A:ASN694 4.0 19.6 1.0 ND1 A:HIS499 4.2 26.3 1.0 ND1 A:HIS690 4.3 18.7 1.0 O A:HOH1443 4.3 49.0 1.0 CG A:HIS499 4.3 19.6 1.0 CG A:HIS690 4.3 18.1 1.0 ND1 A:HIS504 4.4 21.0 1.0 ND2 A:ASN694 4.4 21.2 1.0 CG A:HIS504 4.5 19.1 1.0 CG2 A:ILE837 4.6 20.1 1.0 CA A:ILE839 4.6 22.0 1.0 N A:ILE839 4.9 21.5 1.0 CG2 A:ILE839 4.9 22.5 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