Iron in PDB 1fqe: Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin

The structure of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin, PDB code: 1fqe was solved by D.Nurizzo, H.M.Baker, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.73 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.900, 57.300, 135.900, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.7

The structure of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin (pdb code 1fqe). 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 Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin, PDB code: 1fqe:

Iron binding site 1 out of 1 in the Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:8.0 occ:1.00 OH A:TYR95 2.0 9.2 1.0 OH A:TYR188 2.0 7.9 1.0 OD2 A:ASP63 2.1 8.5 1.0 NE2 A:HIS249 2.2 6.7 1.0 O3 A:CO3600 2.2 9.3 1.0 O2 A:CO3600 2.2 10.1 1.0 C A:CO3600 2.5 9.5 1.0 CZ A:TYR95 3.1 8.4 1.0 CD2 A:HIS249 3.1 6.3 1.0 CZ A:TYR188 3.1 8.5 1.0 CE1 A:HIS249 3.1 7.6 1.0 CG A:ASP63 3.2 6.5 1.0 CE2 A:TYR95 3.7 7.9 1.0 O1 A:CO3600 3.8 10.0 1.0 CB A:ASP63 3.8 6.5 1.0 O A:HOH702 3.9 7.7 1.0 CE2 A:TYR188 3.9 8.3 1.0 CE1 A:TYR188 3.9 9.3 1.0 CE1 A:TYR95 4.1 7.7 1.0 ND1 A:HIS249 4.3 6.7 1.0 CG A:HIS249 4.3 6.6 1.0 OD1 A:ASP63 4.3 6.1 1.0 NZ A:LYS296 4.3 14.0 1.0 CA A:ASP63 4.5 7.2 1.0 CB A:SER125 4.5 6.7 1.0 NH2 A:ARG124 4.5 7.0 1.0 NE A:ARG124 4.7 6.8 1.0 N A:ALA126 4.7 7.7 1.0 N A:SER125 4.8 7.5 1.0 OG A:SER125 4.8 6.4 1.0 CD A:LYS296 4.9 12.6 1.0 CD2 A:TYR95 5.0 8.7 1.0

D.Nurizzo, H.M.Baker, Q.Y.He, R.T.Macgillivray, A.B.Mason, R.C.Woodworth, E.N.Baker. Crystal Structures and Iron Release Properties of Mutants (K206A and K296A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin. Biochemistry V. 40 1616 2001.
ISSN: ISSN 0006-2960
PubMed: 11327820
DOI: 10.1021/BI002050M