Iron in PDB 1b0l: Recombinant Human Diferric Lactoferrin

The structure of Recombinant Human Diferric Lactoferrin, PDB code: 1b0l was solved by E.N.Baker, G.B.Jameson, X.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	156.250, 97.530, 55.870, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 27.4

The binding sites of Iron atom in the Recombinant Human Diferric Lactoferrin (pdb code 1b0l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Recombinant Human Diferric Lactoferrin, PDB code: 1b0l:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Recombinant Human Diferric Lactoferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Human Diferric Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe693 b:27.8 occ:1.00 OH A:TYR192 1.8 24.1 1.0 O1 A:CO3695 2.0 23.0 1.0 OH A:TYR92 2.0 21.3 1.0 NE2 A:HIS253 2.1 21.8 1.0 O2 A:CO3695 2.1 23.0 1.0 OD1 A:ASP60 2.1 33.4 1.0 C A:CO3695 2.4 23.0 1.0 CE1 A:HIS253 3.0 24.2 1.0 CZ A:TYR192 3.1 25.4 1.0 CZ A:TYR92 3.1 24.9 1.0 CD2 A:HIS253 3.1 22.1 1.0 CG A:ASP60 3.3 31.4 1.0 O3 A:CO3695 3.6 23.0 1.0 CE2 A:TYR92 3.7 23.8 1.0 CE1 A:TYR192 3.8 25.4 1.0 O A:HOH1006 3.9 26.9 1.0 CE2 A:TYR192 4.0 25.4 1.0 CE1 A:TYR92 4.1 23.8 1.0 CB A:ASP60 4.1 28.3 1.0 NH2 A:ARG210 4.1 20.1 1.0 OD2 A:ASP60 4.1 33.4 1.0 ND1 A:HIS253 4.2 20.0 1.0 CG A:HIS253 4.2 24.3 1.0 CB A:THR122 4.3 29.1 1.0 NH2 A:ARG121 4.6 31.8 1.0 N A:ALA123 4.6 23.1 1.0 OG1 A:THR122 4.6 26.4 1.0 CA A:ASP60 4.7 27.1 1.0 N A:THR122 4.8 24.0 1.0 CB A:ALA123 4.9 19.4 1.0 NE A:ARG210 5.0 33.6 1.0 NE A:ARG121 5.0 31.2 1.0

Iron binding site 2 out of 2 in the Recombinant Human Diferric Lactoferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Recombinant Human Diferric Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe694 b:21.9 occ:1.00 OH A:TYR528 1.8 25.7 1.0 OH A:TYR435 2.0 19.7 1.0 OD1 A:ASP395 2.0 23.6 1.0 O2 A:CO3696 2.0 20.5 1.0 NE2 A:HIS597 2.2 22.9 1.0 O1 A:CO3696 2.3 20.5 1.0 C A:CO3696 2.5 20.5 1.0 CZ A:TYR528 3.0 25.5 1.0 CZ A:TYR435 3.1 25.0 1.0 CE1 A:HIS597 3.1 24.0 1.0 CG A:ASP395 3.1 26.4 1.0 CD2 A:HIS597 3.2 20.2 1.0 O A:HOH1007 3.6 27.1 1.0 CE2 A:TYR435 3.7 24.7 1.0 O3 A:CO3696 3.7 20.5 1.0 CB A:ASP395 3.8 29.2 1.0 CE1 A:TYR528 3.9 22.6 1.0 CE2 A:TYR528 3.9 22.6 1.0 O A:HOH1004 4.1 33.6 1.0 CE1 A:TYR435 4.1 24.7 1.0 OD2 A:ASP395 4.1 23.6 1.0 ND1 A:HIS597 4.3 22.3 1.0 NH2 A:ARG465 4.3 29.5 1.0 CG A:HIS597 4.4 22.2 1.0 CB A:THR466 4.4 21.9 1.0 CA A:ASP395 4.5 22.2 1.0 N A:ALA467 4.7 27.4 1.0 OG1 A:THR466 4.7 19.4 1.0 N A:THR466 4.8 20.4 1.0 NE A:ARG465 4.8 30.5 1.0 CD2 A:TYR435 5.0 24.3 1.0

X.L.Sun, H.M.Baker, S.C.Shewry, G.B.Jameson, E.N.Baker. Structure of Recombinant Human Lactoferrin Expressed in Aspergillus Awamori. Acta Crystallogr.,Sect.D V. 55 403 1999.
ISSN: ISSN 0907-4449
PubMed: 10089347
DOI: 10.1107/S0907444998011226