Iron in PDB 1dsn: D60S N-Terminal Lobe Human Lactoferrin

The structure of D60S N-Terminal Lobe Human Lactoferrin, PDB code: 1dsn was solved by H.R.Faber, G.E.Norris, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.200, 57.000, 55.200, 90.00, 97.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the D60S N-Terminal Lobe Human Lactoferrin (pdb code 1dsn). 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 D60S N-Terminal Lobe Human Lactoferrin, PDB code: 1dsn:

Iron binding site 1 out of 1 in the D60S 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 D60S N-Terminal Lobe Human Lactoferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:25.0 occ:1.00 OH A:TYR192 1.9 9.8 1.0 OH A:TYR92 1.9 15.5 1.0 O A:HOH750 2.0 20.3 1.0 O2 A:CO3401 2.2 18.6 1.0 NE2 A:HIS253 2.2 26.0 1.0 O1 A:CO3401 2.5 26.8 1.0 C A:CO3401 2.7 53.5 1.0 CZ A:TYR92 2.9 39.7 1.0 CD2 A:HIS253 3.1 26.8 1.0 CZ A:TYR192 3.1 22.3 1.0 CE1 A:HIS253 3.3 27.2 1.0 CE2 A:TYR92 3.3 39.0 1.0 CE1 A:TYR192 3.8 23.5 1.0 O A:HOH749 3.8 26.4 1.0 NH2 A:ARG210 3.8 23.9 1.0 CE1 A:TYR92 3.9 31.7 1.0 O3 A:CO3401 4.0 34.2 1.0 CE2 A:TYR192 4.1 8.9 1.0 OG A:SER60 4.2 41.7 1.0 CG A:HIS253 4.3 25.6 1.0 NH2 A:ARG121 4.3 23.7 1.0 ND1 A:HIS253 4.4 27.3 1.0 CB A:THR122 4.4 38.3 1.0 N A:THR122 4.5 25.0 1.0 CD2 A:TYR92 4.6 39.7 1.0 N A:ALA123 4.7 25.6 1.0 OG1 A:THR122 4.7 35.5 1.0 NE A:ARG121 4.7 20.2 1.0 CZ A:ARG210 4.8 44.3 1.0 CB A:SER60 4.8 43.9 1.0 NE A:ARG210 4.9 19.8 1.0 CA A:THR122 4.9 28.0 1.0

H.R.Faber, T.Bland, C.L.Day, G.E.Norris, J.W.Tweedie, E.N.Baker. Altered Domain Closure and Iron Binding in Transferrins: the Crystal Structure of the ASP60SER Mutant of the Amino-Terminal Half-Molecule of Human Lactoferrin. J.Mol.Biol. V. 256 352 1996.
ISSN: ISSN 0022-2836
PubMed: 8594202
DOI: 10.1006/JMBI.1996.0091