Iron in PDB 1vfe: Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S)

The structure of Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S), PDB code: 1vfe was solved by H.R.Faber, C.L.Day, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.900, 78.800, 58.900, 90.00, 99.20, 90.00
R / Rfree (%)	19.6 / 27.3

The binding sites of Iron atom in the Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S) (pdb code 1vfe). 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 Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S), PDB code: 1vfe:

Iron binding site 1 out of 1 in the Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Lactoferrin, N-Terminal Lobe Mutant with Arg 121 Replaced By Ser (R121S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:20.9 occ:1.00 OH A:TYR192 1.8 22.0 1.0 OH A:TYR92 2.0 12.0 1.0 O1 A:CO3401 2.1 18.0 1.0 OD1 A:ASP60 2.1 7.0 1.0 NE2 A:HIS253 2.3 26.2 1.0 O2 A:CO3401 2.4 7.2 1.0 C A:CO3401 2.5 22.1 1.0 CZ A:TYR192 2.9 30.3 1.0 CZ A:TYR92 3.1 17.2 1.0 CE1 A:HIS253 3.2 26.0 1.0 CG A:ASP60 3.2 17.7 1.0 CD2 A:HIS253 3.3 26.4 1.0 CE2 A:TYR92 3.6 10.7 1.0 O3 A:CO3401 3.7 36.7 1.0 CE1 A:TYR192 3.7 24.3 1.0 CE2 A:TYR192 3.7 28.1 1.0 CE1 A:TYR92 4.0 16.7 1.0 CB A:ASP60 4.1 20.4 1.0 OD2 A:ASP60 4.1 15.9 1.0 O A:HOH542 4.2 50.8 1.0 NH2 A:ARG210 4.2 14.5 1.0 ND1 A:HIS253 4.3 27.0 1.0 CG A:HIS253 4.4 24.3 1.0 CB A:THR122 4.6 20.0 1.0 CA A:ASP60 4.7 20.2 1.0 OG1 A:THR122 4.8 29.8 1.0 CD2 A:TYR92 4.9 12.0 1.0 N A:THR122 4.9 22.6 1.0 N A:ALA123 4.9 16.5 1.0 CD2 A:TYR192 5.0 23.9 1.0

H.R.Faber, C.J.Baker, C.L.Day, J.W.Tweedie, E.N.Baker. Mutation of Arginine 121 in Lactoferrin Destabilizes Iron Binding By Disruption of Anion Binding: Crystal Structures of R121S and R121E Mutants. Biochemistry V. 35 14473 1996.
ISSN: ISSN 0006-2960
PubMed: 8931543
DOI: 10.1021/BI961729G