Iron in PDB 1k7s: Fhud Complexed with Albomycin-Delta 2

The structure of Fhud Complexed with Albomycin-Delta 2, PDB code: 1k7s 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 / 2.60
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	85.570, 85.570, 91.600, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24.3

The binding sites of Iron atom in the Fhud Complexed with Albomycin-Delta 2 (pdb code 1k7s). 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 Fhud Complexed with Albomycin-Delta 2, PDB code: 1k7s:

Iron binding site 1 out of 1 in the Fhud Complexed with Albomycin-Delta 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Fhud Complexed with Albomycin-Delta 2 within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe500 b:40.4 occ:1.00 FE N:ALB500 0.0 40.4 1.0 O7 N:ALB500 2.0 54.1 1.0 O3 N:ALB500 2.0 55.9 1.0 O8 N:ALB500 2.0 43.6 1.0 O6 N:ALB500 2.0 37.5 1.0 O5 N:ALB500 2.0 39.6 1.0 O1 N:ALB500 2.1 42.4 1.0 C3 N:ALB500 2.8 53.6 1.0 N4 N:ALB500 2.8 53.3 1.0 C5 N:ALB500 2.8 36.5 1.0 N5 N:ALB500 2.8 39.8 1.0 C1 N:ALB500 2.8 39.0 1.0 N3 N:ALB500 2.8 41.0 1.0 NH2 N:ARG84 3.9 36.4 1.0 C16 N:ALB500 4.2 50.7 1.0 C17 N:ALB500 4.2 42.5 1.0 C18 N:ALB500 4.2 53.6 1.0 C15 N:ALB500 4.2 43.0 1.0 OH N:TYR106 4.3 32.9 1.0 C10 N:ALB500 4.3 50.2 1.0 N1 N:ALB500 4.3 52.2 1.0 C19 N:ALB500 4.3 39.4 1.0 C20 N:ALB500 4.3 35.6 1.0 N2 N:ALB500 4.3 52.7 1.0 CE1 N:TYR106 4.4 36.8 1.0 NH1 N:ARG84 4.5 36.3 1.0 C11 N:ALB500 4.5 49.0 1.0 C9 N:ALB500 4.6 49.2 1.0 CZ N:ARG84 4.6 37.5 1.0 C12 N:ALB500 4.7 44.4 1.0 C14 N:ALB500 4.7 44.3 1.0 CH2 N:TRP273 4.7 26.1 1.0 CZ N:TYR106 4.7 37.2 1.0 C7 N:ALB500 4.8 50.1 1.0 C13 N:ALB500 4.8 50.0 1.0 C2 N:ALB500 5.0 49.9 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