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Iron in PDB 3r5o: Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution, PDB code: 3r5o was solved by N.Pandey, A.K.Singh, R.P.Singh, M.Sinha, 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) 24.00 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.008, 80.047, 75.676, 90.00, 102.98, 90.00
R / Rfree (%) 21.9 / 24.5

Other elements in 3r5o:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution also contains other interesting chemical elements:

Iodine (I) 10 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution (pdb code 3r5o). 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 Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution, PDB code: 3r5o:

Iron binding site 1 out of 1 in 3r5o

Go back to Iron Binding Sites List in 3r5o
Iron binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A 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 Complex of Bovine Lactoperoxidase with 4- Allyl-2-Methoxyphenol at 2.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:41.5
occ:1.00
 FE A:HEM605 0.0 41.5 1.0
NC A:HEM605 2.0 39.5 1.0
ND A:HEM605 2.0 36.7 1.0
NA A:HEM605 2.1 40.7 1.0
NB A:HEM605 2.2 33.4 1.0
NE2 A:HIS351 2.4 40.1 1.0
O A:HOH753 2.5 59.7 1.0
C4D A:HEM605 3.0 38.3 1.0
C4C A:HEM605 3.0 37.0 1.0
C1D A:HEM605 3.0 37.2 1.0
C1A A:HEM605 3.0 36.9 1.0
C1C A:HEM605 3.1 38.3 1.0
CD2 A:HIS351 3.1 43.2 1.0
C4A A:HEM605 3.1 39.9 1.0
C4B A:HEM605 3.2 36.2 1.0
C1B A:HEM605 3.2 36.9 1.0
CHA A:HEM605 3.3 37.3 1.0
CHD A:HEM605 3.4 37.2 1.0
CHC A:HEM605 3.4 37.6 1.0
CHB A:HEM605 3.5 38.2 1.0
CE1 A:HIS351 3.5 43.4 1.0
C3D A:HEM605 4.3 38.0 1.0
C3C A:HEM605 4.3 39.8 1.0
C2D A:HEM605 4.3 35.4 1.0
C2C A:HEM605 4.3 40.3 1.0
C2A A:HEM605 4.3 36.6 1.0
C3A A:HEM605 4.3 39.0 1.0
CG A:HIS351 4.4 44.8 1.0
O4 A:EUG597 4.4 34.5 0.8
C3B A:HEM605 4.4 34.8 1.0
C2B A:HEM605 4.5 36.0 1.0
NE2 A:GLN105 4.5 32.7 1.0
ND1 A:HIS351 4.5 45.1 1.0
CD2 A:LEU433 4.6 37.2 1.0

Reference:

N.Pandey, A.K.Singh, R.P.Singh, M.Sinha, P.Kaur, S.Sharma, T.P.Singh. Crystal Structure of the Complex of Bovine Lactoperoxidase with 4-Allyl-2-Methoxyphenol at 2.6 A Resolution To Be Published.
Page generated: Sun Aug 4 19:10:18 2024

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