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Iron in PDB 2qqt: Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution, PDB code: 2qqt was solved by A.K.Singh, N.Singh, S.Sharma, P.Kaur, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.44 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.660, 80.520, 77.970, 90.00, 102.65, 90.00
R / Rfree (%) 19.4 / 21.1

Other elements in 2qqt:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution also contains other interesting chemical elements:

Iodine (I) 7 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 Acetyl Salicylic Acid at 2.5 A Resolution (pdb code 2qqt). 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 Acetyl Salicylic Acid at 2.5 A Resolution, PDB code: 2qqt:

Iron binding site 1 out of 1 in 2qqt

Go back to Iron Binding Sites List in 2qqt
Iron binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 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 Acetyl Salicylic Acid at 2.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:17.0
occ:1.00
 FE A:HEM605 0.0 17.0 1.0
NB A:HEM605 2.0 18.5 1.0
ND A:HEM605 2.0 14.3 1.0
NA A:HEM605 2.0 16.7 1.0
NC A:HEM605 2.1 11.6 1.0
NE2 A:HIS351 2.1 17.9 1.0
O A:HOH1025 2.3 24.9 1.0
C4B A:HEM605 3.0 15.8 1.0
C4D A:HEM605 3.0 14.4 1.0
C1B A:HEM605 3.0 19.5 1.0
CD2 A:HIS351 3.0 17.9 1.0
C1A A:HEM605 3.0 17.0 1.0
C1C A:HEM605 3.1 13.3 1.0
C4A A:HEM605 3.1 19.9 1.0
C1D A:HEM605 3.1 11.0 1.0
CE1 A:HIS351 3.2 18.7 1.0
C4C A:HEM605 3.2 12.7 1.0
CHA A:HEM605 3.4 14.8 1.0
CHC A:HEM605 3.4 11.9 1.0
CHB A:HEM605 3.4 19.9 1.0
CHD A:HEM605 3.5 11.3 1.0
CG A:HIS351 4.2 19.9 1.0
ND1 A:HIS351 4.2 18.5 1.0
C2A A:HEM605 4.3 17.7 1.0
C3B A:HEM605 4.3 19.7 1.0
C2C A:HEM605 4.3 11.4 1.0
C3A A:HEM605 4.3 19.3 1.0
C2B A:HEM605 4.3 22.5 1.0
C3D A:HEM605 4.3 13.6 1.0
C3C A:HEM605 4.3 8.2 1.0
C2D A:HEM605 4.4 14.0 1.0
O4 A:AIN596 4.4 64.2 1.0
NE2 A:GLN105 4.5 17.8 1.0
CD2 A:LEU433 5.0 25.0 1.0
NE2 A:HIS109 5.0 16.8 1.0

Reference:

A.K.Singh, N.Singh, S.Sharma, P.Kaur, T.P.Singh. Crystal Structure of the Complex of Bovine Lactoperoxidase with Acetyl Salicylic Acid at 2.5 A Resolution To Be Published.
Page generated: Sun Aug 4 01:50:12 2024

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