Iron in PDB 1eh3: R210K N-Terminal Lobe Human Lactoferrin

The structure of R210K N-Terminal Lobe Human Lactoferrin, PDB code: 1eh3 was solved by N.A.Peterson, B.F.Anderson, G.B.Jameson, J.W.Tweedie, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.440, 57.180, 57.340, 90.00, 117.09, 90.00
R / Rfree (%)	19.8 / 25

The binding sites of Iron atom in the R210K N-Terminal Lobe Human Lactoferrin (pdb code 1eh3). 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 R210K N-Terminal Lobe Human Lactoferrin, PDB code: 1eh3:

Iron binding site 1 out of 1 in the R210K N-Terminal Lobe Human Lactoferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of R210K N-Terminal Lobe Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:13.9 occ:1.00 OH A:TYR192 2.0 9.8 1.0 OD1 A:ASP60 2.1 11.0 1.0 OH A:TYR92 2.1 6.6 1.0 O2 A:CO3401 2.2 11.2 1.0 O1 A:CO3401 2.2 10.7 1.0 NE2 A:HIS253 2.3 11.9 1.0 C A:CO3401 2.5 10.9 1.0 CZ A:TYR92 3.1 9.1 1.0 CD2 A:HIS253 3.1 12.3 1.0 CG A:ASP60 3.2 10.3 1.0 CZ A:TYR192 3.2 9.5 1.0 CE1 A:HIS253 3.4 11.7 1.0 CE2 A:TYR92 3.6 8.3 1.0 O3 A:CO3401 3.7 7.9 1.0 O A:HOH619 3.9 19.1 1.0 CB A:ASP60 3.9 9.3 1.0 CE1 A:TYR192 4.0 8.4 1.0 O A:HOH511 4.1 6.3 1.0 CE1 A:TYR92 4.1 10.8 1.0 CE2 A:TYR192 4.1 8.3 1.0 OD2 A:ASP60 4.1 11.4 1.0 CB A:THR122 4.3 14.1 1.0 CG A:HIS253 4.4 11.6 1.0 NH2 A:ARG121 4.4 8.6 1.0 ND1 A:HIS253 4.4 12.0 1.0 OG1 A:THR122 4.5 15.9 1.0 CA A:ASP60 4.6 11.5 1.0 N A:ALA123 4.7 12.9 1.0 N A:THR122 4.8 13.2 1.0 NE A:ARG121 4.9 13.0 1.0 CD2 A:TYR92 4.9 10.1 1.0

N.A.Peterson, B.F.Anderson, G.B.Jameson, J.W.Tweedie, E.N.Baker. Crystal Structure and Iron-Binding Properties of the R210K Mutant of the N-Lobe of Human Lactoferrin: Implications For Iron Release From Transferrins. Biochemistry V. 39 6625 2000.
ISSN: ISSN 0006-2960
PubMed: 10828980
DOI: 10.1021/BI0001224