Iron in PDB 1bka: Oxalate-Substituted Diferric Lactoferrin

The structure of Oxalate-Substituted Diferric Lactoferrin, PDB code: 1bka was solved by H.M.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)	8.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	155.460, 96.920, 55.850, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / n/a

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

Iron binding site 1 out of 2 in the Oxalate-Substituted Diferric Lactoferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxalate-Substituted Diferric Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe693 b:39.0 occ:1.00 OH A:TYR192 1.6 32.0 1.0 OH A:TYR92 1.9 42.4 1.0 OD1 A:ASP60 1.9 48.5 1.0 O1 A:OXL695 2.0 41.6 1.0 NE2 A:HIS253 2.1 36.9 1.0 O2 A:OXL695 2.3 43.4 1.0 CZ A:TYR192 2.8 36.5 1.0 C1 A:OXL695 2.9 40.0 1.0 CZ A:TYR92 2.9 34.2 1.0 CE1 A:HIS253 3.0 41.0 1.0 C2 A:OXL695 3.0 38.3 1.0 CD2 A:HIS253 3.1 37.7 1.0 CG A:ASP60 3.1 47.8 1.0 O A:HOH916 3.5 52.3 1.0 CE2 A:TYR92 3.6 28.8 1.0 CE1 A:TYR192 3.7 31.5 1.0 CE2 A:TYR192 3.7 30.3 1.0 CE1 A:TYR92 3.9 35.1 1.0 OD2 A:ASP60 3.9 54.5 1.0 O3 A:OXL695 4.1 46.0 1.0 CB A:ASP60 4.1 34.6 1.0 ND1 A:HIS253 4.1 37.1 1.0 NH2 A:ARG210 4.1 23.2 1.0 CG A:HIS253 4.2 30.0 1.0 O4 A:OXL695 4.3 37.2 1.0 CB A:THR122 4.4 32.7 1.0 OG1 A:THR122 4.5 42.9 1.0 CA A:ASP60 4.7 31.0 1.0 N A:ALA123 4.8 20.0 1.0 CD2 A:TYR92 4.9 32.3 1.0 N A:GLY61 4.9 40.8 1.0 CZ A:ARG210 4.9 33.8 1.0 CD1 A:TYR192 4.9 32.8 1.0 NE A:ARG210 5.0 22.5 1.0 CD2 A:TYR192 5.0 37.9 1.0

Iron binding site 2 out of 2 in the Oxalate-Substituted Diferric Lactoferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Oxalate-Substituted Diferric Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe694 b:35.2 occ:1.00 OH A:TYR435 1.6 27.3 1.0 OH A:TYR528 1.8 33.4 1.0 O2 A:OXL696 1.9 20.0 1.0 OD1 A:ASP395 1.9 32.8 1.0 O1 A:OXL696 2.3 19.9 1.0 NE2 A:HIS597 2.3 23.8 1.0 CZ A:TYR435 2.7 27.2 1.0 C2 A:OXL696 2.8 22.9 1.0 CZ A:TYR528 3.0 34.4 1.0 C1 A:OXL696 3.0 33.9 1.0 CG A:ASP395 3.1 48.1 1.0 CE1 A:HIS597 3.2 19.6 1.0 CE1 A:TYR435 3.3 30.4 1.0 CD2 A:HIS597 3.5 25.1 1.0 CE2 A:TYR528 3.8 21.3 1.0 CE2 A:TYR435 3.8 28.9 1.0 CE1 A:TYR528 3.9 18.3 1.0 OD2 A:ASP395 4.0 40.4 1.0 O4 A:OXL696 4.1 29.6 1.0 CB A:ASP395 4.1 34.9 1.0 O A:HOH918 4.2 73.3 1.0 O3 A:OXL696 4.3 31.4 1.0 ND1 A:HIS597 4.4 20.2 1.0 CG A:HIS597 4.5 17.8 1.0 CA A:ASP395 4.6 29.4 1.0 CD1 A:TYR435 4.7 22.6 1.0 N A:ALA467 4.7 33.4 1.0 CB A:THR466 4.8 26.6 1.0 OG1 A:THR466 4.9 34.8 1.0 CB A:ALA467 4.9 24.9 1.0 N A:THR466 4.9 28.1 1.0 CD2 A:TYR435 5.0 22.2 1.0

H.M.Baker, B.F.Anderson, A.M.Brodie, M.S.Shongwe, C.A.Smith, E.N.Baker. Anion Binding By Transferrins: Importance of Second-Shell Effects Revealed By the Crystal Structure of Oxalate-Substituted Diferric Lactoferrin. Biochemistry V. 35 9007 1996.
ISSN: ISSN 0006-2960
PubMed: 8703903
DOI: 10.1021/BI960288Y