Iron in PDB 1dtg: Human Transferrin N-Lobe Mutant H249E

The structure of Human Transferrin N-Lobe Mutant H249E, PDB code: 1dtg was solved by R.T.Macgillivray, M.C.Bewley, C.A.Smith, Q.Y.He, A.B.Mason, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.40
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	72.660, 72.660, 152.490, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 29.4

The binding sites of Iron atom in the Human Transferrin N-Lobe Mutant H249E (pdb code 1dtg). 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 Human Transferrin N-Lobe Mutant H249E, PDB code: 1dtg:

Iron binding site 1 out of 1 in the Human Transferrin N-Lobe Mutant H249E


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Transferrin N-Lobe Mutant H249E within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:43.0 occ:1.00 OH A:TYR95 1.6 40.1 1.0 OH A:TYR188 1.6 39.3 1.0 O2 A:CO3401 2.0 31.6 1.0 O1 A:CO3401 2.0 27.8 1.0 OE2 A:GLU249 2.1 42.3 1.0 OD1 A:ASP63 2.1 27.2 1.0 C A:CO3401 2.4 32.7 1.0 CZ A:TYR95 2.8 37.4 1.0 CZ A:TYR188 2.9 33.6 1.0 CD A:GLU249 3.2 42.8 1.0 CG A:ASP63 3.3 35.5 1.0 CE2 A:TYR95 3.4 42.0 1.0 O A:HOH402 3.5 35.0 1.0 CG A:GLU249 3.6 41.7 1.0 CE1 A:TYR188 3.7 34.0 1.0 O3 A:CO3401 3.7 27.4 1.0 CE2 A:TYR188 3.8 34.9 1.0 CE1 A:TYR95 3.9 38.5 1.0 CB A:ASP63 3.9 35.5 1.0 O A:HOH446 3.9 37.3 1.0 NH1 A:ARG124 4.1 25.9 1.0 OE1 A:GLU249 4.3 42.1 1.0 OD2 A:ASP63 4.3 33.6 1.0 CA A:ASP63 4.5 33.9 1.0 NE A:ARG124 4.6 32.2 1.0 CB A:SER125 4.6 33.8 1.0 CD2 A:TYR95 4.7 42.3 1.0 OG A:SER125 4.7 34.6 1.0 CZ A:ARG124 4.8 33.2 1.0 N A:ALA126 4.9 38.3 1.0 N A:SER125 4.9 30.6 1.0 CD1 A:TYR188 5.0 30.7 1.0

R.T.Macgillivray, M.C.Bewley, C.A.Smith, Q.Y.He, A.B.Mason. Mutation of the Iron Ligand His 249 to Glu in the N-Lobe of Human Transferrin Abolishes the Dilysine "Trigger" But Does Not Significantly Affect Iron Release. Biochemistry V. 39 1211 2000.
ISSN: ISSN 0006-2960
PubMed: 10684598
DOI: 10.1021/BI991522Y