Iron in PDB 1oqh: Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin

The structure of Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin, PDB code: 1oqh was solved by H.M.Baker, Q.-Y.He, S.K.Brigg, A.B.Mason, E.N Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.930, 57.120, 135.250, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 28.8

The structure of Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin (pdb code 1oqh). 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 Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin, PDB code: 1oqh:

Iron binding site 1 out of 1 in the Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the R124A Mutant of the N-Lobe Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:20.7 occ:1.00 OH A:TYR95 2.0 23.4 1.0 O2 A:CO3600 2.0 20.6 1.0 OH A:TYR188 2.1 20.8 1.0 OD1 A:ASP63 2.1 19.7 1.0 O3 A:CO3600 2.2 20.6 1.0 NE2 A:HIS249 2.4 19.7 1.0 C A:CO3600 2.4 20.7 1.0 CD2 A:HIS249 3.1 19.1 1.0 CZ A:TYR95 3.1 22.9 1.0 CG A:ASP63 3.3 19.9 1.0 CZ A:TYR188 3.3 21.1 1.0 CE1 A:HIS249 3.5 19.5 1.0 CE2 A:TYR95 3.6 22.9 1.0 O1 A:CO3600 3.7 20.5 1.0 O A:HOH771 3.7 20.2 1.0 CB A:ASP63 3.8 20.1 1.0 CE1 A:TYR188 4.1 20.9 1.0 CE1 A:TYR95 4.1 23.0 1.0 CE2 A:TYR188 4.2 21.0 1.0 OD2 A:ASP63 4.3 19.9 1.0 NZ A:LYS296 4.3 17.3 1.0 CG A:HIS249 4.3 18.8 1.0 CA A:ASP63 4.4 20.0 1.0 ND1 A:HIS249 4.5 19.1 1.0 CB A:SER125 4.7 21.6 1.0 N A:ALA126 4.8 21.2 1.0 CD2 A:TYR95 4.9 23.3 1.0 CE A:LYS296 4.9 18.1 1.0 OG A:SER125 4.9 21.9 1.0 CD A:LYS296 5.0 18.1 1.0

H.M.Baker, Q.-Y.He, S.K.Briggs, A.B.Mason, E.N.Baker. Structural and Functional Consequences of Binding Site Mutations in Transferrin: Crystal Structures of the ASP63GLU and ARG124ALA Mutants of the N-Lobe of Human Transferrin Biochemistry V. 42 7084 2003.
ISSN: ISSN 0006-2960
PubMed: 12795604
DOI: 10.1021/BI020689F