Cerium in PDB 1fck: Structure of Diceric Human Lactoferrin

The structure of Structure of Diceric Human Lactoferrin, PDB code: 1fck was solved by H.M.Baker, C.J.Baker, C.A.Smith, E.N.Baker, 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 (°)	154.900, 97.100, 56.000, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 25.7

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

Cerium binding site 1 out of 2 in the Structure of Diceric Human Lactoferrin


Mono view


Stereo pair view

A full contact list of Cerium with other atoms in the Ce binding site number 1 of Structure of Diceric Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ce693 b:48.5 occ:0.58 OH A:TYR192 2.2 38.1 1.0 OH A:TYR92 2.3 37.8 1.0 OD1 A:ASP60 2.5 37.9 1.0 NE2 A:HIS253 2.6 28.7 1.0 O2 A:CO3695 2.6 39.1 1.0 O3 A:CO3695 2.7 32.5 1.0 C A:CO3695 3.0 36.3 1.0 CZ A:TYR92 3.2 35.6 1.0 CD2 A:HIS253 3.3 29.1 1.0 CZ A:TYR192 3.3 34.1 1.0 CG A:ASP60 3.5 33.5 1.0 CE1 A:HIS253 3.6 31.3 1.0 CE2 A:TYR92 3.8 31.2 1.0 O A:HOH700 3.8 32.1 1.0 CE1 A:TYR192 3.9 34.0 1.0 CB A:ASP60 3.9 31.9 1.0 CE1 A:TYR92 4.1 34.6 1.0 NH2 A:ARG210 4.1 27.9 1.0 O1 A:CO3695 4.3 41.2 1.0 CB A:THR122 4.3 28.7 1.0 CE2 A:TYR192 4.3 33.1 1.0 OD2 A:ASP60 4.4 37.0 1.0 OG1 A:THR122 4.5 27.4 1.0 CA A:ASP60 4.5 29.6 1.0 CG A:HIS253 4.6 29.7 1.0 ND1 A:HIS253 4.7 30.8 1.0 NH2 A:ARG121 4.7 29.9 1.0 N A:ALA123 4.7 28.6 1.0 N A:THR122 4.9 31.9 1.0 N A:GLY61 4.9 29.8 1.0 CD2 A:TYR92 5.0 31.4 1.0

Cerium binding site 2 out of 2 in the Structure of Diceric Human Lactoferrin


Mono view


Stereo pair view

A full contact list of Cerium with other atoms in the Ce binding site number 2 of Structure of Diceric Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ce694 b:43.5 occ:0.57 OH A:TYR528 2.2 25.8 1.0 OD1 A:ASP395 2.3 29.1 1.0 OH A:TYR435 2.3 31.0 1.0 O1 A:CO3696 2.5 27.2 1.0 O2 A:CO3696 2.6 28.6 1.0 NE2 A:HIS597 2.8 28.4 1.0 C A:CO3696 2.9 30.8 1.0 CG A:ASP395 3.2 28.3 1.0 CZ A:TYR528 3.2 25.3 1.0 CZ A:TYR435 3.2 32.6 1.0 CE2 A:TYR435 3.6 30.8 1.0 CD2 A:HIS597 3.6 25.8 1.0 CE1 A:TYR528 3.7 26.1 1.0 O A:HOH703 3.8 26.9 1.0 CE1 A:HIS597 3.9 25.4 1.0 OD2 A:ASP395 3.9 30.0 1.0 CB A:ASP395 4.0 26.6 1.0 O3 A:CO3696 4.1 32.4 1.0 O A:HOH855 4.2 24.7 1.0 CE2 A:TYR528 4.2 25.5 1.0 CE1 A:TYR435 4.3 32.1 1.0 CB A:THR466 4.3 27.5 1.0 NH2 A:ARG465 4.3 29.0 1.0 N A:ALA467 4.5 27.1 1.0 OG1 A:THR466 4.6 26.6 1.0 CA A:ASP395 4.7 27.6 1.0 N A:THR466 4.7 27.7 1.0 NE A:ARG465 4.8 26.6 1.0 CG A:HIS597 4.8 27.0 1.0 CD2 A:TYR435 4.9 31.4 1.0 CB A:ALA467 4.9 26.1 1.0 ND1 A:HIS597 4.9 23.8 1.0 CA A:THR466 5.0 26.8 1.0

H.M.Baker, C.J.Baker, C.A.Smith, E.N.Baker. Metal Substitution in Transferrins: Specific Binding of Cerium(IV) Revealed By the Crystal Structure of Cerium-Substituted Human Lactoferrin. J.Biol.Inorg.Chem. V. 5 692 2000.
ISSN: ISSN 0949-8257
PubMed: 11128996
DOI: 10.1007/S007750000157