Iron in PDB 1h43: R210E N-Terminal Lobe Human Lactoferrin

The structure of R210E N-Terminal Lobe Human Lactoferrin, PDB code: 1h43 was solved by N.A.Peterson, V.L.Arcus, 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)	30.00 / 2.2
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	112.900, 57.900, 57.800, 90.00, 101.40, 90.00
R / Rfree (%)	20.3 / 23.5

The binding sites of Iron atom in the R210E N-Terminal Lobe Human Lactoferrin (pdb code 1h43). 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 R210E N-Terminal Lobe Human Lactoferrin, PDB code: 1h43:

Iron binding site 1 out of 1 in the R210E 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 R210E N-Terminal Lobe Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1315 b:29.0 occ:1.00 OH A:TYR192 2.0 25.2 1.0 OH A:TYR92 2.1 32.0 1.0 OD1 A:ASP60 2.1 24.9 1.0 O1 A:CO31314 2.1 27.6 1.0 NE2 A:HIS253 2.2 30.9 1.0 O2 A:CO31314 2.5 30.6 1.0 C A:CO31314 2.7 29.5 1.0 CZ A:TYR92 3.1 30.4 1.0 CD2 A:HIS253 3.1 28.6 1.0 CG A:ASP60 3.2 28.8 1.0 CZ A:TYR192 3.2 23.5 1.0 CE1 A:HIS253 3.2 28.5 1.0 CE2 A:TYR92 3.6 29.1 1.0 O A:HOH2022 3.8 24.2 1.0 CB A:ASP60 3.9 29.7 1.0 CE1 A:TYR192 3.9 23.1 1.0 O3 A:CO31314 4.0 25.0 1.0 OD2 A:ASP60 4.1 30.4 1.0 CE2 A:TYR192 4.1 24.9 1.0 CE1 A:TYR92 4.1 28.8 1.0 CG A:HIS253 4.3 28.2 1.0 ND1 A:HIS253 4.3 29.9 1.0 CE A:LYS301 4.3 26.3 1.0 NZ A:LYS301 4.5 26.3 1.0 CA A:ASP60 4.5 30.8 1.0 CB A:THR122 4.6 25.6 1.0 N A:ALA123 4.8 24.6 1.0 NH2 A:ARG121 4.8 32.3 1.0 N A:THR122 4.9 24.5 1.0 CD2 A:TYR92 4.9 28.6 1.0 OG1 A:THR122 4.9 25.7 1.0 N A:GLY61 5.0 33.2 1.0

N.A.Peterson, V.L.Arcus, B.F.Anderson, J.W.Tweedie, G.B.Jameson, E.N.Baker. "Dilysine Trigger" in Transferrins Probed By Mutagenesis of Lactoferrin: Crystal Structures of the R210G, R210E, and R210L Mutants of Human Lactoferrin Biochemistry V. 41 14167 2002.
ISSN: ISSN 0006-2960
PubMed: 12450380
DOI: 10.1021/BI020443A