Iron in PDB 2g93: Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution

The structure of Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution, PDB code: 2g93 was solved by N.Singh, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.411, 50.439, 65.956, 90.00, 107.76, 90.00
R / Rfree (%)	18.8 / 22.9

The structure of Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution (pdb code 2g93). 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 Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution, PDB code: 2g93:

Iron binding site 1 out of 1 in the Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D- Mannopyranoside at 1.9 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe688 b:18.7 occ:1.00 OH A:TYR526 1.9 17.2 1.0 OH A:TYR433 2.0 18.7 1.0 O2 A:CO3689 2.0 18.6 1.0 OD1 A:ASP395 2.1 14.8 1.0 O1 A:CO3689 2.1 19.4 1.0 NE2 A:HIS595 2.2 15.6 1.0 C A:CO3689 2.4 18.7 1.0 CZ A:TYR433 3.0 17.5 1.0 CZ A:TYR526 3.1 16.9 1.0 CG A:ASP395 3.2 15.9 1.0 CD2 A:HIS595 3.2 15.4 1.0 CE1 A:HIS595 3.2 16.9 1.0 CE1 A:TYR433 3.6 19.1 1.0 O3 A:CO3689 3.7 18.5 1.0 CB A:ASP395 3.8 15.5 1.0 CE1 A:TYR526 3.8 16.0 1.0 O A:HOH710 3.9 18.0 1.0 CE2 A:TYR526 3.9 15.4 1.0 O A:HOH704 4.0 20.1 1.0 CE2 A:TYR433 4.0 18.4 1.0 OD2 A:ASP395 4.1 16.8 1.0 ND1 A:HIS595 4.3 17.4 1.0 CG A:HIS595 4.3 17.8 1.0 NH2 A:ARG463 4.3 23.8 1.0 CB A:THR464 4.4 17.6 1.0 CA A:ASP395 4.5 16.1 1.0 N A:ALA465 4.7 17.9 1.0 NE A:ARG463 4.8 19.4 1.0 N A:THR464 4.8 17.0 1.0 OG1 A:THR464 4.8 16.4 1.0 CD1 A:TYR433 4.9 19.5 1.0

N.Singh, S.Sharma, T.P.Singh. Ligand Recognition Site in C-Lobe of Lactoferrin: Crystal Structure of the Complex of C-Lobe of Bovine Lactoferrin with Methyl Alpha-D-Mannopyranoside at 1.9 A Resolution To Be Published.