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Iron in PDB 2pt3: Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites

Enzymatic activity of Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites

All present enzymatic activity of Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites, PDB code: 2pt3 was solved by A.K.Singh, N.Singh, S.Sharma, P.Kaur, C.Betzel, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.38 / 2.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.910, 80.051, 75.675, 90.00, 103.23, 90.00
R / Rfree (%) 23.1 / 24.7

Other elements in 2pt3:

The structure of Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites (pdb code 2pt3). 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 Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites, PDB code: 2pt3:

Iron binding site 1 out of 1 in 2pt3

Go back to Iron Binding Sites List in 2pt3
Iron binding site 1 out of 1 in the Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites


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 Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe623

b:37.4
occ:1.00
 FE A:HEM623 0.0 37.4 1.0
NB A:HEM623 1.9 34.0 1.0
NC A:HEM623 2.0 36.2 1.0
ND A:HEM623 2.0 34.6 1.0
NA A:HEM623 2.1 35.4 1.0
NE2 A:HIS351 2.3 32.2 1.0
O A:HOH748 2.7 40.3 1.0
C4B A:HEM623 2.9 34.2 1.0
C1B A:HEM623 3.0 35.3 1.0
C4C A:HEM623 3.0 34.9 1.0
C1C A:HEM623 3.0 32.1 1.0
C1D A:HEM623 3.0 37.7 1.0
C4A A:HEM623 3.1 38.5 1.0
C4D A:HEM623 3.1 36.1 1.0
CD2 A:HIS351 3.2 35.4 1.0
C1A A:HEM623 3.2 36.5 1.0
CHC A:HEM623 3.3 30.3 1.0
CHD A:HEM623 3.3 37.2 1.0
CE1 A:HIS351 3.4 39.4 1.0
CHB A:HEM623 3.4 37.8 1.0
CHA A:HEM623 3.6 36.2 1.0
C3B A:HEM623 4.1 29.1 1.0
C2B A:HEM623 4.2 33.1 1.0
O1 A:PO4607 4.2 51.9 1.0
C2C A:HEM623 4.2 37.1 1.0
C3C A:HEM623 4.2 37.0 1.0
C2D A:HEM623 4.3 34.5 1.0
C3D A:HEM623 4.3 35.2 1.0
C3A A:HEM623 4.4 40.9 1.0
CG A:HIS351 4.4 38.5 1.0
C2A A:HEM623 4.4 40.9 1.0
ND1 A:HIS351 4.4 37.1 1.0
NE2 A:GLN105 4.5 36.2 1.0
CG A:GLN105 4.8 40.7 1.0
CD2 A:LEU433 4.8 38.2 1.0
O3 A:PO4607 5.0 55.5 1.0

Reference:

A.K.Singh, N.Singh, S.Sharma, M.Perbandt, P.Kaur, C.Betzel, A.Srinivasan, T.P.Singh. Crystal Structure of Bovine Lactoperoxidase at 2.34 A Resolution Reveals Multiple Anion Binding Sites To Be Published.
Page generated: Sun Aug 4 01:29:51 2024

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