Iron in PDB 3qlb: Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin

The structure of Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin, PDB code: 3qlb was solved by K.Brillet, S.Noel, G.L.A.Mislin, C.Reimmann, I.J.Schalk, D.Cobessi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.57 / 3.26
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	155.070, 170.830, 232.620, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.9

The binding sites of Iron atom in the Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin (pdb code 3qlb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin, PDB code: 3qlb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:64.9 occ:1.00 FE3 A:EFE701 0.0 64.9 1.0 N1 A:EFE701 1.9 63.8 1.0 O1 A:EFE701 1.9 64.3 1.0 O21 A:EFE701 2.0 64.9 1.0 N2 A:EFE701 2.0 64.4 1.0 O2 A:CIT700 2.0 66.8 1.0 O4 A:CIT700 2.1 70.2 1.0 C18 A:EFE701 2.4 64.9 1.0 C12 A:EFE701 2.8 62.4 1.0 C1 A:EFE701 2.9 61.8 1.0 C19 A:EFE701 2.9 65.0 1.0 C14 A:EFE701 3.0 63.4 1.0 C17 A:EFE701 3.0 64.4 1.0 C15 A:EFE701 3.0 63.5 1.0 C1 A:CIT700 3.0 70.1 1.0 C6 A:EFE701 3.2 61.7 1.0 C5 A:CIT700 3.4 76.6 1.0 C2 A:CIT700 3.4 74.1 1.0 C4 A:CIT700 4.0 79.2 1.0 O1 A:CIT700 4.1 70.6 1.0 C2 A:EFE701 4.1 60.8 1.0 O20 A:EFE701 4.2 65.1 1.0 C16 A:EFE701 4.3 62.9 1.0 C13 A:EFE701 4.3 62.5 1.0 C3 A:CIT700 4.3 80.3 1.0 CG A:PRO244 4.4 69.1 1.0 O3 A:CIT700 4.4 77.1 1.0 S1 A:EFE701 4.4 61.7 1.0 CB A:PRO244 4.5 68.7 1.0 C5 A:EFE701 4.6 60.6 1.0 S2 A:EFE701 4.6 61.6 1.0 CG A:ARG245 4.7 73.9 1.0 CZ A:PHE331 4.8 59.0 1.0 O7 A:CIT700 5.0 81.4 1.0

Iron binding site 2 out of 2 in the Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Enantiopyochelin Outer Membrane Tonb-Dependent Transporter From Pseudomonas Fluorescens Bound to the Ferri-Enantiopyochelin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:69.6 occ:1.00 FE3 B:EFE701 0.0 69.6 1.0 O1 B:EFE701 1.9 71.1 1.0 N1 B:EFE701 2.0 70.7 1.0 O21 B:EFE701 2.0 68.8 1.0 O2 B:CIT700 2.0 73.0 1.0 N2 B:EFE701 2.0 68.7 1.0 O4 B:CIT700 2.1 75.4 1.0 C18 B:EFE701 2.4 67.7 1.0 C19 B:EFE701 2.9 68.0 1.0 C12 B:EFE701 2.9 70.5 1.0 C14 B:EFE701 2.9 69.4 1.0 C17 B:EFE701 3.0 68.0 1.0 C1 B:EFE701 3.0 70.5 1.0 C15 B:EFE701 3.0 68.4 1.0 C1 B:CIT700 3.0 76.8 1.0 C6 B:EFE701 3.3 69.4 1.0 C5 B:CIT700 3.5 80.6 1.0 C2 B:CIT700 3.6 81.2 1.0 O1 B:CIT700 3.9 76.9 1.0 O20 B:EFE701 4.2 67.2 1.0 C2 B:EFE701 4.2 70.3 1.0 CB B:PRO244 4.3 67.6 1.0 CG B:PRO244 4.3 67.6 1.0 C16 B:EFE701 4.3 67.5 1.0 C13 B:EFE701 4.3 69.4 1.0 O3 B:CIT700 4.3 81.2 1.0 C3 B:CIT700 4.5 85.7 1.0 S1 B:EFE701 4.5 70.7 1.0 C4 B:CIT700 4.6 82.6 1.0 S2 B:EFE701 4.6 67.5 1.0 O7 B:CIT700 4.6 87.5 1.0 CZ B:PHE331 4.6 59.9 1.0 C5 B:EFE701 4.7 68.2 1.0 CG B:ARG245 4.7 73.8 1.0 NH1 B:ARG245 4.8 90.0 1.0

K.Brillet, C.Reimmann, G.L.A.Mislin, S.Noel, D.Rognan, I.J.Schalk, D.Cobessi. Pyochelin Enantiomers and Their Outer-Membrane Siderophore Transporters in Fluorescent Pseudomonads: Structural Bases For Unique Enantiospecific Recognition J.Am.Chem.Soc. V. 133 16503 2011.
ISSN: ISSN 0002-7863
PubMed: 21902256
DOI: 10.1021/JA205504Z