Iron in PDB 5hbc: Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination

The structure of Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination, PDB code: 5hbc was solved by A.Singh, N.Rastogi, P.K.Singh, T.K.Tyagi, P.Kaur, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.45 / 2.79
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	159.654, 82.580, 107.694, 90.00, 128.08, 90.00
R / Rfree (%)	20.6 / 27.3

The binding sites of Iron atom in the Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination (pdb code 5hbc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination, PDB code: 5hbc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe704 b:86.8 occ:1.00 O2 A:BCT705 2.1 54.9 1.0 O1 A:BCT705 2.1 58.7 1.0 OH A:TYR433 2.2 93.5 1.0 OH A:TYR526 2.3 62.1 1.0 OD2 A:ASP395 2.3 56.6 1.0 C A:BCT705 2.4 57.8 1.0 NE2 A:HIS595 2.9 45.8 1.0 CZ A:TYR526 3.2 52.5 1.0 CZ A:TYR433 3.3 83.3 1.0 O A:HOH801 3.4 49.7 1.0 CG A:ASP395 3.4 47.7 1.0 CD2 A:HIS595 3.6 42.2 1.0 O3 A:BCT705 3.7 49.1 1.0 CE1 A:TYR526 3.8 53.4 1.0 CE2 A:TYR433 4.0 81.9 1.0 CE1 A:HIS595 4.0 43.3 1.0 CB A:ASP395 4.1 45.8 1.0 CE2 A:TYR526 4.2 51.0 1.0 NH2 A:ARG463 4.2 57.2 1.0 CE1 A:TYR433 4.3 80.6 1.0 CB A:THR464 4.4 58.5 1.0 OD1 A:ASP395 4.4 56.9 1.0 N A:ALA465 4.6 58.8 1.0 CA A:ASP395 4.6 42.1 1.0 N A:THR464 4.7 53.2 1.0 NE A:ARG463 4.7 53.3 1.0 CG A:HIS595 4.9 42.1 1.0 CZ A:ARG463 4.9 59.0 1.0 OG1 A:THR464 4.9 53.1 1.0

Iron binding site 2 out of 2 in the Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Intermediate Structure of Iron-Saturated C-Lobe of Bovine Lactoferrin at 2.79 Angstrom Resolution Indicates the Softening of Iron Coordination within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe706 b:65.9 occ:1.00 OD2 B:ASP395 2.0 54.3 1.0 OH B:TYR526 2.1 56.9 1.0 O2 B:BCT707 2.1 46.1 1.0 OH B:TYR433 2.2 68.1 1.0 O1 B:BCT707 2.2 42.6 1.0 C B:BCT707 2.5 48.0 1.0 NE2 B:HIS595 2.9 45.8 1.0 CZ B:TYR526 3.1 52.8 1.0 CG B:ASP395 3.1 47.3 1.0 CZ B:TYR433 3.2 69.0 1.0 CE2 B:TYR433 3.7 63.2 1.0 CB B:ASP395 3.7 45.0 1.0 CD2 B:HIS595 3.7 41.0 1.0 O3 B:BCT707 3.8 42.7 1.0 CE1 B:TYR526 3.8 51.4 1.0 CE1 B:HIS595 3.8 45.8 1.0 O B:HOH801 3.9 52.8 1.0 CE2 B:TYR526 4.0 51.5 1.0 OD1 B:ASP395 4.2 49.7 1.0 CE1 B:TYR433 4.2 73.6 1.0 NH1 B:ARG463 4.3 46.8 1.0 CB B:THR464 4.3 55.4 1.0 O B:HOH803 4.4 44.4 1.0 CA B:ASP395 4.4 39.2 1.0 N B:ALA465 4.6 55.5 1.0 N B:THR464 4.6 55.2 1.0 NE B:ARG463 4.6 54.4 1.0 OG1 B:THR464 4.8 52.3 1.0 CZ B:ARG463 4.9 47.2 1.0 CG B:HIS595 4.9 41.2 1.0 CA B:THR464 4.9 56.5 1.0 ND1 B:HIS595 5.0 46.5 1.0 N B:GLY396 5.0 42.1 1.0 CD2 B:TYR433 5.0 70.1 1.0

N.Rastogi, A.Singh, P.K.Singh, T.K.Tyagi, S.Pandey, K.Shin, P.Kaur, S.Sharma, T.P.Singh. Structure of Iron Saturated C-Lobe of Bovine Lactoferrin at pH 6.8 Indicates A Weakening of Iron Coordination Proteins V. 84 591 2016.
ISSN: ESSN 1097-0134
PubMed: 26850578
DOI: 10.1002/PROT.25004