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Iron in PDB 5gls: Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety

Enzymatic activity of Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety

All present enzymatic activity of Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety:
1.11.1.7;

Protein crystallography data

The structure of Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety, PDB code: 5gls was solved by P.Tiwari, P.K.Singh, H.V.Sirohi, 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) 50.00 / 1.93
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.005, 79.834, 76.126, 90.00, 102.30, 90.00
R / Rfree (%) 19.2 / 24.5

Other elements in 5gls:

The structure of Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety also contains other interesting chemical elements:

Iodine (I) 18 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety (pdb code 5gls). 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 Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety, PDB code: 5gls:

Iron binding site 1 out of 1 in 5gls

Go back to Iron Binding Sites List in 5gls
Iron binding site 1 out of 1 in the Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bovine Lactoperoxidase with A Partially Modified Covalent Bond with Heme Moiety within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe707

b:21.3
occ:1.00
 FE A:HEM707 0.0 21.3 1.0
ND A:HEM707 1.9 20.7 1.0
NE2 A:HIS351 2.0 19.6 1.0
NA A:HEM707 2.1 19.7 1.0
NC A:HEM707 2.1 19.8 1.0
NB A:HEM707 2.1 18.0 1.0
I A:IOD709 2.7 66.5 0.4
C1D A:HEM707 2.9 19.5 1.0
C4D A:HEM707 2.9 19.4 1.0
CD2 A:HIS351 2.9 20.2 1.0
CE1 A:HIS351 3.0 21.0 1.0
C4C A:HEM707 3.0 17.4 1.0
C1A A:HEM707 3.0 20.4 1.0
C4B A:HEM707 3.1 21.4 1.0
C1C A:HEM707 3.1 18.9 1.0
C4A A:HEM707 3.1 21.3 1.0
C1B A:HEM707 3.1 20.1 1.0
CHD A:HEM707 3.3 17.2 1.0
CHA A:HEM707 3.4 19.9 1.0
CHC A:HEM707 3.5 19.3 1.0
CHB A:HEM707 3.5 18.6 1.0
ND1 A:HIS351 4.1 19.7 1.0
CG A:HIS351 4.1 19.5 1.0
C2D A:HEM707 4.2 17.3 1.0
C3D A:HEM707 4.2 20.4 1.0
C3C A:HEM707 4.3 19.8 1.0
C2A A:HEM707 4.3 21.3 1.0
NE2 A:GLN105 4.3 19.6 1.0
C2C A:HEM707 4.3 20.4 1.0
C3A A:HEM707 4.4 22.0 1.0
C2B A:HEM707 4.4 17.9 1.0
C3B A:HEM707 4.4 21.1 1.0
CD2 A:LEU433 4.8 18.4 1.0
O A:HOH801 4.9 16.5 0.7

Reference:

P.K.Singh, H.V.Sirohi, N.Iqbal, P.Tiwari, P.Kaur, S.Sharma, T.P.Singh. Structure of Bovine Lactoperoxidase with A Partially Linked Heme Moiety at 1.98 Angstrom Resolution Biochim. Biophys. Acta V.1865 329 2016.
ISSN: ISSN 0006-3002
PubMed: 27986533
DOI: 10.1016/J.BBAPAP.2016.12.006
Page generated: Sun Dec 13 16:02:25 2020

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