Iron in PDB 2ikc: Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate

All present enzymatic activity of Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate:
1.11.1.7;

The structure of Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate, PDB code: 2ikc was solved by I.A.Sheikh, N.Singh, A.K.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)	19.97 / 3.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	59.080, 72.590, 84.470, 85.20, 84.07, 75.41
R / Rfree (%)	18.7 / 23

The structure of Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Iron atom in the Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate (pdb code 2ikc). 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 Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate, PDB code: 2ikc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate


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 Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe605 b:7.8 occ:1.00 FE A:HEM605 0.0 7.8 1.0 ND A:HEM605 2.0 3.2 1.0 NB A:HEM605 2.1 4.2 1.0 NC A:HEM605 2.2 3.2 1.0 NE2 A:HIS351 2.2 2.0 1.0 NA A:HEM605 2.2 2.0 1.0 C4D A:HEM605 2.9 3.6 1.0 CD2 A:HIS351 2.9 2.0 1.0 C1A A:HEM605 3.0 2.0 1.0 C4B A:HEM605 3.0 2.9 1.0 C1D A:HEM605 3.1 3.6 1.0 C1C A:HEM605 3.1 2.7 1.0 C1B A:HEM605 3.2 3.0 1.0 CHA A:HEM605 3.2 3.2 1.0 C4C A:HEM605 3.3 2.0 1.0 CE1 A:HIS351 3.3 2.9 1.0 C4A A:HEM605 3.3 2.0 1.0 CHC A:HEM605 3.4 2.0 1.0 CHD A:HEM605 3.6 2.3 1.0 CHB A:HEM605 3.7 2.1 1.0 O2 A:FMT3003 3.7 17.3 1.0 CG A:HIS351 4.1 2.0 1.0 C3D A:HEM605 4.2 3.5 1.0 C3B A:HEM605 4.3 3.2 1.0 ND1 A:HIS351 4.3 2.1 1.0 C2D A:HEM605 4.3 3.7 1.0 C2A A:HEM605 4.3 2.0 1.0 C2B A:HEM605 4.3 2.9 1.0 C2C A:HEM605 4.4 3.1 1.0 C A:FMT3003 4.5 19.8 1.0 C3C A:HEM605 4.5 2.0 1.0 C3A A:HEM605 4.5 2.0 1.0 NE2 A:GLN105 4.5 2.8 1.0 CD2 A:LEU433 4.8 2.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate


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 Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe605 b:12.5 occ:1.00 FE B:HEM605 0.0 12.5 1.0 ND B:HEM605 2.0 12.3 1.0 NB B:HEM605 2.0 13.7 1.0 NC B:HEM605 2.2 13.1 1.0 NA B:HEM605 2.2 10.6 1.0 NE2 B:HIS351 2.4 2.0 1.0 C4D B:HEM605 2.9 13.0 1.0 C4B B:HEM605 2.9 13.3 1.0 C1A B:HEM605 3.0 10.1 1.0 C1C B:HEM605 3.1 11.4 1.0 C1B B:HEM605 3.1 12.4 1.0 C1D B:HEM605 3.2 11.6 1.0 CHA B:HEM605 3.2 11.3 1.0 CD2 B:HIS351 3.3 2.0 1.0 CHC B:HEM605 3.3 12.6 1.0 C4C B:HEM605 3.3 12.2 1.0 C4A B:HEM605 3.3 11.1 1.0 CE1 B:HIS351 3.4 2.8 1.0 O1 B:FMT3006 3.6 18.7 1.0 CHB B:HEM605 3.7 12.2 1.0 CHD B:HEM605 3.7 11.5 1.0 C B:FMT3006 4.0 19.2 1.0 C3B B:HEM605 4.2 13.7 1.0 NE2 B:GLN105 4.2 3.4 1.0 C3D B:HEM605 4.2 14.1 1.0 C2B B:HEM605 4.3 12.7 1.0 C2A B:HEM605 4.3 9.6 1.0 C2D B:HEM605 4.3 12.7 1.0 C2C B:HEM605 4.4 11.0 1.0 CG B:HIS351 4.5 2.1 1.0 ND1 B:HIS351 4.5 2.7 1.0 C3A B:HEM605 4.5 10.0 1.0 C3C B:HEM605 4.5 11.5 1.0 CD2 B:LEU433 4.9 2.0 1.0

I.A.Sheikh, N.Singh, A.K.Singh, S.Sharma, T.P.Singh. Crystal Structure of Sheep Lactoperoxidase at 3.25 A Resolution Reveals the Binding Sites For Formate To Be Published.