Iron in PDB 1qff: E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron

The structure of E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron, PDB code: 1qff was solved by A.D.Ferguson, E.Hofmann, J.W.Coulton, K.Diederichs, W.Welte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.70
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	171.400, 171.400, 85.700, 90.00, 90.00, 120.00
R / Rfree (%)	23.1 / 27.6

The binding sites of Iron atom in the E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron (pdb code 1qff). 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 E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron, PDB code: 1qff:

Iron binding site 1 out of 1 in the E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E. Coli Ferric Hydroxamate Uptake Receptor (Fhua) in Complex with Bound Ferrichrome-Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1050 b:45.1 occ:1.00 FE A:FCI1050 0.0 45.1 1.0 O14 A:FCI1050 2.0 48.5 1.0 O11 A:FCI1050 2.1 42.7 1.0 O8 A:FCI1050 2.1 54.1 1.0 O6 A:FCI1050 2.1 53.8 1.0 O10 A:FCI1050 2.1 43.6 1.0 O3 A:FCI1050 2.2 37.8 1.0 C6 A:FCI1050 2.8 50.6 1.0 N6 A:FCI1050 2.8 48.5 1.0 C9 A:FCI1050 2.8 54.4 1.0 N8 A:FCI1050 2.8 48.5 1.0 C3 A:FCI1050 2.9 47.9 1.0 N5 A:FCI1050 2.9 52.3 1.0 C21 A:FCI1050 4.1 48.0 1.0 C32 A:FCI1050 4.2 37.5 1.0 N1 A:FCI1050 4.2 49.0 1.0 C35 A:FCI1050 4.2 40.3 1.0 C34 A:FCI1050 4.2 47.8 1.0 N3 A:FCI1050 4.2 49.9 1.0 CE2 A:TYR244 4.2 27.5 1.0 C37 A:FCI1050 4.3 36.2 1.0 C30 A:FCI1050 4.3 42.8 1.0 NH2 A:ARG81 4.3 52.4 1.0 C36 A:FCI1050 4.3 54.2 1.0 OH A:TYR116 4.3 47.8 1.0 CZ2 A:TRP246 4.4 49.9 1.0 CE1 A:TYR116 4.4 46.9 1.0 NH1 A:ARG81 4.4 52.2 1.0 C13 A:FCI1050 4.5 49.9 1.0 OH A:TYR244 4.5 42.3 1.0 NE1 A:TRP246 4.5 51.7 1.0 C25 A:FCI1050 4.6 34.6 1.0 C24 A:FCI1050 4.7 39.4 1.0 C29 A:FCI1050 4.7 40.4 1.0 C27 A:FCI1050 4.7 45.1 1.0 C4 A:FCI1050 4.7 45.8 1.0 CZ A:TYR244 4.8 25.7 1.0 CE2 A:TRP246 4.8 42.2 1.0 CZ A:ARG81 4.8 48.0 1.0 C18 A:FCI1050 4.8 37.4 1.0 CZ A:TYR116 4.9 46.5 1.0 CG A:GLN100 4.9 47.9 1.0

A.D.Ferguson, W.Welte, E.Hofmann, B.Lindner, O.Holst, J.W.Coulton, K.Diederichs. A Conserved Structural Motif For Lipopolysaccharide Recognition By Procaryotic and Eucaryotic Proteins. Structure Fold.Des. V. 8 585 2000.
ISSN: ISSN 0969-2126
PubMed: 10873859
DOI: 10.1016/S0969-2126(00)00143-X