Iron in PDB 1lfg: Structure of Diferric Human Lactoferrin

The structure of Structure of Diferric Human Lactoferrin, PDB code: 1lfg was solved by E.N.Baker, B.F.Anderson, M.Haridas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	156.260, 97.400, 55.850, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

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

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Diferric Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe693 b:30.4 occ:1.00 OH A:TYR192 1.9 29.0 1.0 OD1 A:ASP60 1.9 28.0 1.0 O1 A:CO3695 2.1 30.9 1.0 NE2 A:HIS253 2.1 27.9 1.0 O2 A:CO3695 2.1 32.3 1.0 OH A:TYR92 2.2 30.4 1.0 C A:CO3695 2.4 27.3 1.0 CD2 A:HIS253 3.1 29.2 1.0 CE1 A:HIS253 3.1 34.9 1.0 CZ A:TYR192 3.1 33.9 1.0 CZ A:TYR92 3.1 23.7 1.0 CG A:ASP60 3.1 34.2 1.0 CE2 A:TYR92 3.6 19.5 1.0 O3 A:CO3695 3.7 32.9 1.0 CE1 A:TYR192 3.8 35.0 1.0 CB A:ASP60 3.9 29.8 1.0 CE2 A:TYR192 4.1 27.0 1.0 O A:HOH962 4.1 33.3 1.0 OD2 A:ASP60 4.1 32.1 1.0 CE1 A:TYR92 4.1 19.3 1.0 NH2 A:ARG210 4.2 20.5 1.0 CG A:HIS253 4.2 34.8 1.0 ND1 A:HIS253 4.3 25.4 1.0 CB A:THR122 4.4 29.9 1.0 NH2 A:ARG121 4.6 27.8 1.0 OG1 A:THR122 4.7 29.1 1.0 CA A:ASP60 4.7 31.9 1.0 N A:ALA123 4.7 26.9 1.0 CD2 A:TYR92 4.9 22.8 1.0 N A:THR122 4.9 33.2 1.0 NE A:ARG121 4.9 33.7 1.0

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Diferric Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe694 b:28.2 occ:1.00 OH A:TYR435 1.9 30.4 1.0 O2 A:CO3696 2.0 26.7 1.0 OH A:TYR528 2.0 24.6 1.0 O1 A:CO3696 2.1 26.6 1.0 OD1 A:ASP395 2.1 37.1 1.0 NE2 A:HIS597 2.1 21.9 1.0 C A:CO3696 2.4 22.4 1.0 CE1 A:HIS597 2.9 19.9 1.0 CZ A:TYR435 2.9 37.1 1.0 CZ A:TYR528 3.1 24.8 1.0 CG A:ASP395 3.2 35.1 1.0 CE2 A:TYR435 3.3 36.0 1.0 CD2 A:HIS597 3.3 25.1 1.0 O3 A:CO3696 3.7 25.9 1.0 O A:HOH964 3.9 29.4 1.0 CE1 A:TYR528 3.9 20.8 1.0 CB A:ASP395 4.0 22.6 1.0 CE2 A:TYR528 4.0 19.4 1.0 O A:HOH965 4.0 28.4 1.0 CE1 A:TYR435 4.0 25.8 1.0 ND1 A:HIS597 4.1 18.2 1.0 OD2 A:ASP395 4.2 30.4 1.0 CG A:HIS597 4.3 19.2 1.0 CA A:ASP395 4.5 29.1 1.0 NE A:ARG465 4.5 38.3 1.0 NH2 A:ARG465 4.5 38.2 1.0 CB A:THR466 4.6 31.7 1.0 N A:ALA467 4.6 29.4 1.0 CD2 A:TYR435 4.6 32.1 1.0 N A:THR466 4.8 26.9 1.0 CZ A:ARG465 4.8 42.0 1.0 OG1 A:THR466 4.9 29.9 1.0

M.Haridas, B.F.Anderson, E.N.Baker. Structure of Human Diferric Lactoferrin Refined at 2.2 A Resolution. Acta Crystallogr.,Sect.D V. 51 629 1995.
ISSN: ISSN 0907-4449
PubMed: 15299793
DOI: 10.1107/S0907444994013521