Iron in PDB 7equ: Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution

The structure of Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution, PDB code: 7equ was solved by A.Maurya, J.Singh, A.Sharma, P.Sharma, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.85 / 2.74
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	153.759, 81.554, 111.364, 90, 129.95, 90
R / Rfree (%)	23.9 / 29.8

The binding sites of Iron atom in the Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution (pdb code 7equ). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution, PDB code: 7equ:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution


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 C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:99.8 occ:1.00 OH A:TYR433 2.0 108.8 1.0 OD2 A:ASP395 2.0 107.5 1.0 OH A:TYR526 2.1 79.5 1.0 O2 A:BCT702 2.1 83.3 1.0 O1 A:BCT702 2.1 64.8 1.0 NE2 A:HIS595 2.3 81.0 1.0 C A:BCT702 2.3 79.2 1.0 CG A:ASP395 3.1 84.6 1.0 CZ A:TYR526 3.1 71.9 1.0 CD2 A:HIS595 3.2 64.4 1.0 CZ A:TYR433 3.2 119.4 1.0 CE1 A:HIS595 3.3 72.4 1.0 O A:HOH801 3.4 94.4 1.0 O3 A:BCT702 3.6 58.4 1.0 O A:HOH805 3.8 69.3 1.0 CB A:ASP395 3.8 76.5 1.0 CE2 A:TYR433 3.9 118.4 1.0 CE1 A:TYR526 3.9 68.8 1.0 CE2 A:TYR526 4.0 71.4 1.0 OD1 A:ASP395 4.0 104.8 1.0 CE1 A:TYR433 4.2 118.7 1.0 CG A:HIS595 4.4 56.9 1.0 CA A:ASP395 4.4 68.1 1.0 ND1 A:HIS595 4.4 61.3 1.0 NH2 A:ARG463 4.5 82.3 1.0 NE A:ARG463 4.6 89.6 1.0 CB A:THR464 4.7 96.4 1.0 N A:GLY396 4.8 82.7 1.0 N A:THR464 4.8 88.8 1.0 N A:ALA465 4.8 96.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution


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 the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:86.2 occ:1.00 O2 B:BCT702 2.0 55.1 1.0 NE2 B:HIS595 2.0 55.7 1.0 O3 B:BCT702 2.0 46.0 1.0 OH B:TYR433 2.1 95.2 1.0 OD2 B:ASP395 2.1 98.3 1.0 OH B:TYR526 2.2 74.8 1.0 C B:BCT702 2.3 61.6 1.0 CG B:ASP395 2.9 71.4 1.0 CZ B:TYR433 3.0 114.3 1.0 CD2 B:HIS595 3.0 53.3 1.0 CE1 B:HIS595 3.1 50.6 1.0 CZ B:TYR526 3.2 55.1 1.0 O B:HOH801 3.5 51.8 1.0 O1 B:BCT702 3.6 57.8 1.0 CE2 B:TYR433 3.6 113.0 1.0 OD1 B:ASP395 3.7 74.6 1.0 CB B:ASP395 3.7 64.0 1.0 CE1 B:TYR433 3.9 121.6 1.0 CE2 B:TYR526 3.9 56.0 1.0 CE1 B:TYR526 4.0 58.3 1.0 CG B:HIS595 4.1 44.3 1.0 ND1 B:HIS595 4.2 47.0 1.0 CA B:ASP395 4.2 60.7 1.0 CB B:THR464 4.5 79.1 1.0 NH1 B:ARG463 4.5 71.8 1.0 N B:ALA465 4.7 91.5 1.0 NE B:ARG463 4.8 97.5 1.0 N B:THR464 4.8 70.1 1.0 N B:GLY396 4.8 82.7 1.0 CD2 B:TYR433 4.8 120.8 1.0

A.Maurya, J.Singh, A.Sharma, P.Sharma, S.Sharma, T.P.Singh. Crystal Structure of the C-Lobe of Lactoferrin Produced By Limited Proteolysis Using Pepsin at 2.74A Resolution To Be Published.