Iron in PDB 4wha: Lipoxygenase-1 (Soybean) L546A/L754A Mutant

All present enzymatic activity of Lipoxygenase-1 (Soybean) L546A/L754A Mutant:
1.13.11.12;

The structure of Lipoxygenase-1 (Soybean) L546A/L754A Mutant, PDB code: 4wha was solved by A.D.Scouras, C.A.M.Carr, S.Hu, J.P.Klinman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.03 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	94.126, 92.644, 49.572, 90.00, 90.34, 90.00
R / Rfree (%)	13.7 / 17.9

The binding sites of Iron atom in the Lipoxygenase-1 (Soybean) L546A/L754A Mutant (pdb code 4wha). 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) L546A/L754A Mutant, PDB code: 4wha:

Iron binding site 1 out of 1 in the Lipoxygenase-1 (Soybean) L546A/L754A 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) L546A/L754A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:19.7 occ:0.57 O A:HOH1352 2.1 29.4 1.0 NE2 A:HIS499 2.2 26.0 0.8 NE2 A:HIS504 2.2 22.6 1.0 NE2 A:HIS690 2.3 17.9 1.0 OXT A:ILE839 2.3 26.2 1.0 HE2 A:HIS499 2.4 40.1 0.2 OD1 A:ASN694 2.4 20.9 0.3 HE1 A:HIS499 2.7 22.0 0.2 NE2 A:HIS499 2.7 33.4 0.2 CE1 A:HIS499 2.9 18.4 0.2 CE1 A:HIS499 3.0 37.3 0.8 HE1 A:HIS499 3.0 44.8 0.8 CE1 A:HIS504 3.2 23.0 1.0 OD1 A:ASN694 3.2 20.3 0.7 CE1 A:HIS690 3.2 16.9 1.0 CD2 A:HIS690 3.2 20.6 1.0 CD2 A:HIS504 3.3 21.4 1.0 CD2 A:HIS499 3.3 21.1 0.8 HE1 A:HIS504 3.3 27.6 1.0 C A:ILE839 3.3 34.5 1.0 HD2 A:HIS690 3.4 24.7 1.0 HE1 A:HIS690 3.4 20.3 1.0 HD2 A:HIS504 3.4 25.7 1.0 CG A:ASN694 3.5 36.8 0.3 O A:ILE839 3.5 25.0 1.0 HD2 A:HIS499 3.5 25.3 0.8 CG A:ASN694 3.7 13.5 0.7 HB2 A:ASN694 3.7 20.2 0.7 HG23 A:ILE837 3.7 22.2 1.0 HB2 A:ASN694 3.7 16.6 0.3 CD2 A:HIS499 3.8 20.8 0.2 ND1 A:HIS499 4.0 17.1 0.2 ND1 A:HIS499 4.2 34.5 0.8 CB A:ASN694 4.2 13.9 0.3 CB A:ASN694 4.2 16.8 0.7 H12 A:EDO906 4.3 67.0 1.0 H A:ILE839 4.3 26.6 1.0 HG23 A:ILE839 4.3 31.9 1.0 ND1 A:HIS504 4.3 20.6 1.0 CG A:HIS499 4.3 19.9 0.8 HD2 A:HIS499 4.4 24.9 0.2 ND1 A:HIS690 4.4 19.4 1.0 CG A:HIS504 4.4 22.2 1.0 ND2 A:ASN694 4.4 14.8 0.7 H21 A:EDO906 4.4 66.8 1.0 CG A:HIS690 4.4 17.2 1.0 ND2 A:ASN694 4.4 23.7 0.3 HD21 A:ASN694 4.5 28.4 0.3 HD21 A:ASN694 4.5 17.8 0.7 CG A:HIS499 4.5 25.6 0.2 H22 A:EDO906 4.5 66.8 1.0 CG2 A:ILE837 4.5 18.5 1.0 HG22 A:ILE837 4.6 22.2 1.0 O A:HOH1424 4.7 29.6 0.8 CA A:ILE839 4.7 20.7 1.0 HB1 A:ALA754 4.7 23.2 1.0 HG21 A:ILE837 4.8 22.2 1.0 HB3 A:ASN694 4.8 16.6 0.3 HE22 A:GLN697 4.8 27.2 1.0 HB3 A:ASN694 4.8 20.2 0.7 C2 A:EDO906 4.9 55.6 1.0 N A:ILE839 4.9 22.2 1.0 HD1 A:HIS499 4.9 41.5 0.8 HA A:ASN694 5.0 20.8 0.3 HD22 A:ASN694 5.0 17.8 0.7

S.Hu, S.C.Sharma, A.D.Scouras, A.V.Soudackov, C.A.Carr, S.Hammes-Schiffer, T.Alber, J.P.Klinman. Extremely Elevated Room-Temperature Kinetic Isotope Effects Quantify the Critical Role of Barrier Width in Enzymatic C-H Activation. J.Am.Chem.Soc. V. 136 8157 2014.
ISSN: ESSN 1520-5126
PubMed: 24884374
DOI: 10.1021/JA502726S