Iron in PDB 2o7u: Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin

The structure of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin, PDB code: 2o7u was solved by H.M.Baker, D.Nurizzo, 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)	29.76 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	169.462, 97.897, 208.953, 90.00, 90.01, 90.00
R / Rfree (%)	23 / 25.9

The binding sites of Iron atom in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin (pdb code 2o7u). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 9 binding sites of Iron where determined in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin, PDB code: 2o7u:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Iron binding site 1 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of 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 K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:39.4 occ:1.00 OH B:TYR95 1.8 53.6 1.0 OD1 B:ASP63 1.9 53.4 1.0 NE2 B:HIS249 2.0 55.1 1.0 OH B:TYR188 2.1 55.7 1.0 O3 B:CO3600 2.1 45.0 1.0 O2 B:CO3600 2.2 43.4 1.0 C B:CO3600 2.5 44.6 1.0 CZ B:TYR95 2.9 54.6 1.0 CD2 B:HIS249 3.0 55.5 1.0 CG B:ASP63 3.0 53.1 1.0 CE1 B:HIS249 3.0 55.5 1.0 CZ B:TYR188 3.1 57.6 1.0 CE2 B:TYR95 3.5 54.9 1.0 O B:HOH602 3.6 38.1 1.0 CB B:ASP63 3.6 54.0 1.0 O1 B:CO3600 3.8 44.5 1.0 CE2 B:TYR188 3.8 56.1 1.0 CE1 B:TYR95 3.9 56.3 1.0 CE1 B:TYR188 4.0 58.1 1.0 O B:HOH603 4.0 32.8 1.0 NH2 B:ARG124 4.1 64.7 1.0 OD2 B:ASP63 4.1 52.8 1.0 ND1 B:HIS249 4.1 57.1 1.0 CG B:HIS249 4.2 55.5 1.0 CA B:ASP63 4.3 54.0 1.0 CB B:SER125 4.4 57.4 1.0 NE B:ARG124 4.6 57.9 1.0 N B:SER125 4.7 56.9 1.0 N B:ALA126 4.8 57.3 1.0 CZ B:ARG124 4.8 60.9 1.0 CD2 B:TYR95 4.8 54.4 1.0

Iron binding site 2 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:39.3 occ:1.00 OH A:TYR95 1.8 53.8 1.0 OD1 A:ASP63 1.9 53.5 1.0 NE2 A:HIS249 2.0 55.2 1.0 O3 A:CO3600 2.2 44.8 1.0 OH A:TYR188 2.2 56.0 1.0 O2 A:CO3600 2.2 43.3 1.0 C A:CO3600 2.5 44.4 1.0 CD2 A:HIS249 3.0 55.6 1.0 CE1 A:HIS249 3.0 55.5 1.0 CZ A:TYR95 3.0 54.7 1.0 CG A:ASP63 3.0 52.9 1.0 CZ A:TYR188 3.1 57.6 1.0 CB A:ASP63 3.5 54.2 1.0 CE2 A:TYR95 3.6 54.5 1.0 CE2 A:TYR188 3.8 56.0 1.0 O1 A:CO3600 3.8 44.5 1.0 O A:HOH602 3.9 33.7 1.0 NH2 A:ARG124 4.0 64.5 1.0 CE1 A:TYR95 4.0 56.5 1.0 CE1 A:TYR188 4.0 58.2 1.0 OD2 A:ASP63 4.1 52.4 1.0 ND1 A:HIS249 4.1 56.8 1.0 CG A:HIS249 4.1 55.6 1.0 CA A:ASP63 4.3 54.0 1.0 CB A:SER125 4.4 57.4 1.0 O A:HOH603 4.5 29.4 1.0 NE A:ARG124 4.6 57.8 1.0 N A:SER125 4.7 57.0 1.0 CZ A:ARG124 4.7 60.8 1.0 N A:ALA126 4.8 57.3 1.0 CD2 A:TYR95 5.0 54.1 1.0 CD2 A:TYR188 5.0 54.3 1.0

Iron binding site 3 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:39.4 occ:1.00 OH C:TYR95 1.8 53.6 1.0 OD1 C:ASP63 1.9 53.3 1.0 NE2 C:HIS249 2.0 55.3 1.0 OH C:TYR188 2.1 56.0 1.0 O3 C:CO3600 2.1 45.0 1.0 O2 C:CO3600 2.2 43.4 1.0 C C:CO3600 2.5 44.5 1.0 CZ C:TYR95 3.0 54.5 1.0 CD2 C:HIS249 3.0 55.7 1.0 CE1 C:HIS249 3.0 55.5 1.0 CG C:ASP63 3.0 52.9 1.0 CZ C:TYR188 3.1 57.4 1.0 CB C:ASP63 3.5 54.2 1.0 CE2 C:TYR95 3.6 54.5 1.0 CE2 C:TYR188 3.7 55.9 1.0 O1 C:CO3600 3.8 44.4 1.0 O C:HOH603 3.8 31.5 1.0 CE1 C:TYR95 4.0 56.5 1.0 NH2 C:ARG124 4.0 64.6 1.0 CE1 C:TYR188 4.0 58.1 1.0 OD2 C:ASP63 4.0 52.7 1.0 ND1 C:HIS249 4.1 56.9 1.0 CG C:HIS249 4.1 55.8 1.0 O C:HOH607 4.3 33.8 1.0 CA C:ASP63 4.3 54.1 1.0 CB C:SER125 4.5 57.5 1.0 NE C:ARG124 4.6 57.7 1.0 CZ C:ARG124 4.7 60.6 1.0 N C:SER125 4.8 56.9 1.0 N C:ALA126 4.8 57.3 1.0 CD2 C:TYR95 4.9 54.4 1.0 CD2 C:TYR188 4.9 54.3 1.0

Iron binding site 4 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:44.3 occ:1.00 OH D:TYR188 1.9 57.0 1.0 OD1 D:ASP63 1.9 57.9 1.0 OH D:TYR95 2.0 56.2 1.0 NE2 D:HIS249 2.1 56.6 1.0 O3 D:CO3600 2.2 49.7 1.0 O2 D:CO3600 2.2 49.9 1.0 C D:CO3600 2.6 50.2 1.0 CZ D:TYR188 3.0 57.8 1.0 CG D:ASP63 3.0 57.1 1.0 CZ D:TYR95 3.1 55.5 1.0 CE1 D:HIS249 3.1 56.9 1.0 CD2 D:HIS249 3.1 56.5 1.0 O D:HOH603 3.4 23.5 1.0 CB D:ASP63 3.5 56.1 1.0 CE2 D:TYR95 3.6 54.9 1.0 CE1 D:TYR188 3.8 57.9 1.0 O1 D:CO3600 3.8 50.6 1.0 CE2 D:TYR188 3.8 58.5 1.0 CE1 D:TYR95 4.1 55.4 1.0 OD2 D:ASP63 4.1 57.7 1.0 ND1 D:HIS249 4.2 57.0 1.0 CG D:HIS249 4.3 56.5 1.0 CB D:SER125 4.3 56.5 1.0 CA D:ASP63 4.3 55.7 1.0 NH2 D:ARG124 4.3 57.4 1.0 O D:HOH606 4.3 22.9 1.0 N D:SER125 4.6 57.0 1.0 NE D:ARG124 4.7 56.9 1.0 N D:ALA126 4.7 56.7 1.0 OG D:SER125 4.7 56.5 1.0 CD2 D:TYR95 4.9 55.3 1.0 CZ D:ARG124 5.0 57.4 1.0

Iron binding site 5 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe500 b:44.0 occ:1.00 OH E:TYR188 1.9 57.1 1.0 OH E:TYR95 2.0 56.3 1.0 OD1 E:ASP63 2.0 57.8 1.0 NE2 E:HIS249 2.1 56.4 1.0 O2 E:CO3600 2.1 49.9 1.0 O3 E:CO3600 2.3 49.7 1.0 C E:CO3600 2.6 50.1 1.0 CG E:ASP63 3.0 57.2 1.0 CZ E:TYR188 3.0 57.9 1.0 CZ E:TYR95 3.0 55.4 1.0 CE1 E:HIS249 3.1 57.0 1.0 CD2 E:HIS249 3.1 56.3 1.0 CB E:ASP63 3.5 56.1 1.0 O E:HOH604 3.5 15.4 1.0 CE2 E:TYR95 3.6 54.9 1.0 O1 E:CO3600 3.8 50.6 1.0 CE2 E:TYR188 3.8 58.5 1.0 CE1 E:TYR188 3.9 57.9 1.0 O E:HOH605 4.0 22.5 1.0 CE1 E:TYR95 4.1 55.3 1.0 OD2 E:ASP63 4.2 57.7 1.0 ND1 E:HIS249 4.2 57.0 1.0 CG E:HIS249 4.2 56.4 1.0 CA E:ASP63 4.3 55.7 1.0 NH2 E:ARG124 4.3 57.3 1.0 CB E:SER125 4.4 56.5 1.0 NE E:ARG124 4.7 56.9 1.0 N E:SER125 4.7 57.1 1.0 N E:ALA126 4.8 56.7 1.0 OG E:SER125 4.8 56.5 1.0 CD2 E:TYR95 4.9 55.3 1.0 CZ E:ARG124 5.0 57.4 1.0

Iron binding site 6 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe500 b:43.6 occ:1.00 OH F:TYR95 1.9 56.1 1.0 OH F:TYR188 1.9 57.0 1.0 OD1 F:ASP63 1.9 57.8 1.0 NE2 F:HIS249 2.1 56.3 1.0 O3 F:CO3600 2.2 49.8 1.0 O2 F:CO3600 2.2 49.9 1.0 C F:CO3600 2.5 50.2 1.0 CZ F:TYR95 3.0 55.5 1.0 CG F:ASP63 3.0 57.2 1.0 CZ F:TYR188 3.0 57.9 1.0 CD2 F:HIS249 3.1 56.3 1.0 CE1 F:HIS249 3.1 56.9 1.0 O F:HOH603 3.2 18.1 1.0 CB F:ASP63 3.5 56.2 1.0 CE2 F:TYR95 3.6 55.0 1.0 O1 F:CO3600 3.8 50.6 1.0 O F:HOH605 3.9 31.4 1.0 CE2 F:TYR188 3.9 58.5 1.0 CE1 F:TYR188 3.9 58.0 1.0 CE1 F:TYR95 4.1 55.5 1.0 OD2 F:ASP63 4.1 57.6 1.0 ND1 F:HIS249 4.2 56.9 1.0 CG F:HIS249 4.3 56.4 1.0 CA F:ASP63 4.3 55.6 1.0 CB F:SER125 4.4 56.5 1.0 NH2 F:ARG124 4.4 57.5 1.0 N F:SER125 4.6 57.0 1.0 NE F:ARG124 4.7 56.8 1.0 N F:ALA126 4.7 56.7 1.0 OG F:SER125 4.8 56.5 1.0 CD2 F:TYR95 4.9 55.3 1.0 N F:ALA64 5.0 54.4 1.0

Iron binding site 7 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe500 b:44.3 occ:1.00 OH G:TYR188 1.8 57.3 1.0 OH G:TYR95 2.1 56.1 1.0 OD1 G:ASP63 2.1 57.8 1.0 NE2 G:HIS249 2.2 56.5 1.0 O3 G:CO3600 2.2 49.6 1.0 O2 G:CO3600 2.2 50.0 1.0 C G:CO3600 2.6 50.1 1.0 CZ G:TYR188 2.9 57.9 1.0 CZ G:TYR95 3.1 55.4 1.0 CE1 G:HIS249 3.1 56.9 1.0 CG G:ASP63 3.2 57.0 1.0 CD2 G:HIS249 3.2 56.5 1.0 CE2 G:TYR95 3.6 55.0 1.0 CB G:ASP63 3.6 56.2 1.0 CE1 G:TYR188 3.7 57.7 1.0 CE2 G:TYR188 3.8 58.5 1.0 O1 G:CO3600 3.8 50.4 1.0 CE1 G:TYR95 4.1 55.4 1.0 ND1 G:HIS249 4.3 56.9 1.0 NH2 G:ARG124 4.3 57.4 1.0 OD2 G:ASP63 4.3 57.4 1.0 CG G:HIS249 4.3 56.5 1.0 CA G:ASP63 4.4 55.7 1.0 CB G:SER125 4.5 56.4 1.0 NE G:ARG124 4.6 56.8 1.0 N G:SER125 4.7 56.9 1.0 N G:ALA126 4.8 56.8 1.0 OG G:SER125 4.9 56.6 1.0 CD2 G:TYR95 4.9 55.2 1.0 CZ G:ARG124 4.9 57.6 1.0 O G:HOH601 5.0 51.1 1.0

Iron binding site 8 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe500 b:44.4 occ:1.00 OH H:TYR188 1.9 57.2 1.0 OH H:TYR95 2.1 56.0 1.0 OD1 H:ASP63 2.1 57.7 1.0 O2 H:CO3600 2.1 50.0 1.0 NE2 H:HIS249 2.2 56.5 1.0 O3 H:CO3600 2.3 49.5 1.0 C H:CO3600 2.5 50.1 1.0 CZ H:TYR188 3.0 58.0 1.0 CZ H:TYR95 3.1 55.4 1.0 CG H:ASP63 3.1 57.0 1.0 CE1 H:HIS249 3.1 56.8 1.0 CD2 H:HIS249 3.2 56.5 1.0 CB H:ASP63 3.6 56.3 1.0 CE2 H:TYR95 3.6 55.0 1.0 O1 H:CO3600 3.8 50.6 1.0 CE1 H:TYR188 3.8 57.8 1.0 CE2 H:TYR188 3.8 58.5 1.0 CE1 H:TYR95 4.1 55.5 1.0 OD2 H:ASP63 4.2 57.4 1.0 NH2 H:ARG124 4.2 57.5 1.0 ND1 H:HIS249 4.3 57.0 1.0 CG H:HIS249 4.3 56.5 1.0 CA H:ASP63 4.4 55.7 1.0 CB H:SER125 4.4 56.6 1.0 NE H:ARG124 4.6 56.9 1.0 N H:SER125 4.6 56.8 1.0 N H:ALA126 4.7 56.9 1.0 OG H:SER125 4.8 56.7 1.0 O H:HOH602 4.9 37.8 1.0 CZ H:ARG124 4.9 57.5 1.0 CD2 H:TYR95 4.9 55.2 1.0

Iron binding site 9 out of 9 in the Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of K206E/K296E Mutant of the N-Terminal Half Molecule of Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe500 b:43.7 occ:1.00 OH I:TYR188 1.9 57.3 1.0 OH I:TYR95 2.1 56.1 1.0 OD1 I:ASP63 2.1 57.7 1.0 O3 I:CO3600 2.1 49.5 1.0 NE2 I:HIS249 2.2 56.6 1.0 O2 I:CO3600 2.2 50.0 1.0 C I:CO3600 2.5 50.0 1.0 CZ I:TYR188 3.0 58.0 1.0 CZ I:TYR95 3.1 55.4 1.0 CE1 I:HIS249 3.1 56.8 1.0 CG I:ASP63 3.1 56.9 1.0 CD2 I:HIS249 3.1 56.5 1.0 CB I:ASP63 3.6 56.2 1.0 O I:HOH602 3.6 41.7 1.0 CE2 I:TYR95 3.6 55.0 1.0 O1 I:CO3600 3.7 50.6 1.0 CE1 I:TYR188 3.8 57.8 1.0 CE2 I:TYR188 3.8 58.5 1.0 CE1 I:TYR95 4.2 55.4 1.0 NH2 I:ARG124 4.2 57.4 1.0 ND1 I:HIS249 4.2 56.8 1.0 OD2 I:ASP63 4.3 57.3 1.0 CG I:HIS249 4.3 56.5 1.0 CA I:ASP63 4.4 55.7 1.0 CB I:SER125 4.5 56.5 1.0 NE I:ARG124 4.6 56.8 1.0 N I:SER125 4.7 56.9 1.0 N I:ALA126 4.8 56.9 1.0 O I:HOH603 4.8 52.1 1.0 OG I:SER125 4.9 56.6 1.0 CZ I:ARG124 4.9 57.5 1.0 CD2 I:TYR95 4.9 55.2 1.0

H.M.Baker, D.Nurizzo, A.B.Mason, E.N.Baker. Structures of Two Mutants That Probe the Role in Iron Release of the Dilysine Pair in the N-Lobe of Human Transferrin. Acta Crystallogr.,Sect.D V. 63 408 2007.
ISSN: ISSN 0907-4449
PubMed: 17327678
DOI: 10.1107/S0907444907000182