Iron in PDB 1esz: Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen

The structure of Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen, PDB code: 1esz was solved by T.E.Clarke, V.Braun, G.Winkelmann, L.W.Tari, H.J.Vogel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	86.090, 86.090, 91.940, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 24.1

The binding sites of Iron atom in the Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen (pdb code 1esz). 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 Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen, PDB code: 1esz:

Iron binding site 1 out of 1 in the Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Periplasmic Ferric Siderophore Binding Protein Fhud Complexed with Coprogen within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:23.4 occ:1.00 FE A:CPO500 0.0 23.4 1.0 O11 A:CPO500 2.0 25.6 1.0 O7 A:CPO500 2.0 25.8 1.0 O12 A:CPO500 2.0 24.5 1.0 O2 A:CPO500 2.0 24.8 1.0 O3 A:CPO500 2.0 24.1 1.0 O8 A:CPO500 2.1 26.0 1.0 C28 A:CPO500 2.7 26.6 1.0 N5 A:CPO500 2.7 27.6 1.0 N4 A:CPO500 2.7 28.2 1.0 C6 A:CPO500 2.8 23.9 1.0 N1 A:CPO500 2.8 24.2 1.0 C17 A:CPO500 2.8 28.2 1.0 C27 A:CPO500 4.0 29.6 1.0 OH A:TYR106 4.0 21.4 1.0 O A:HOH600 4.1 28.0 1.0 C5 A:CPO500 4.2 26.0 1.0 C11 A:CPO500 4.2 28.1 1.0 C29 A:CPO500 4.2 28.9 1.0 CE1 A:TYR275 4.2 19.4 1.0 C16 A:CPO500 4.3 22.9 1.0 C18 A:CPO500 4.3 31.3 1.0 C33 A:CPO500 4.3 29.8 1.0 O13 A:CPO500 4.3 47.0 1.0 NH2 A:ARG84 4.4 25.7 1.0 CE1 A:TYR106 4.6 22.0 1.0 C4 A:CPO500 4.7 27.5 1.0 C24 A:CPO500 4.7 41.1 1.0 CD1 A:TYR275 4.7 18.5 1.0 C26 A:CPO500 4.8 33.8 1.0 CH2 A:TRP273 4.8 20.6 1.0 CZ A:TYR106 4.8 22.6 1.0 C30 A:CPO500 4.9 30.8 1.0 C12 A:CPO500 4.9 22.0 1.0 C9 A:CPO500 5.0 31.4 1.0 NH1 A:ARG84 5.0 26.8 1.0

T.E.Clarke, V.Braun, G.Winkelmann, L.W.Tari, H.J.Vogel. X-Ray Crystallographic Structures of the Escherichia Coli Periplasmic Protein Fhud Bound to Hydroxamate-Type Siderophores and the Antibiotic Albomycin. J.Biol.Chem. V. 277 13966 2002.
ISSN: ISSN 0021-9258
PubMed: 11805094
DOI: 10.1074/JBC.M109385200