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Iron in PDB 2qpk: Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution, PDB code: 2qpk 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) 20.00 / 2.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.618, 80.553, 77.803, 90.00, 102.56, 90.00
R / Rfree (%) 17.2 / 22

Other elements in 2qpk:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution also contains other interesting chemical elements:

Iodine (I) 8 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 Salicylhydroxamic Acid at 2.34 A Resolution (pdb code 2qpk). 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 Salicylhydroxamic Acid at 2.34 A Resolution, PDB code: 2qpk:

Iron binding site 1 out of 1 in 2qpk

Go back to Iron Binding Sites List in 2qpk
Iron binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 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 Salicylhydroxamic Acid at 2.34 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:24.4
occ:1.00
 FE A:HEM605 0.0 24.4 1.0
NC A:HEM605 2.0 21.6 1.0
NA A:HEM605 2.1 22.6 1.0
NB A:HEM605 2.1 22.1 1.0
ND A:HEM605 2.1 20.5 1.0
NE2 A:HIS351 2.2 19.8 1.0
O9 A:SHA616 2.9 36.5 1.0
C4C A:HEM605 3.0 17.6 1.0
C1C A:HEM605 3.0 19.1 1.0
C4B A:HEM605 3.0 20.4 1.0
C1A A:HEM605 3.0 20.8 1.0
CD2 A:HIS351 3.0 18.1 1.0
C1D A:HEM605 3.1 17.5 1.0
C4D A:HEM605 3.1 15.8 1.0
C1B A:HEM605 3.1 21.9 1.0
C4A A:HEM605 3.1 23.3 1.0
CE1 A:HIS351 3.2 18.8 1.0
CHC A:HEM605 3.4 18.8 1.0
CHD A:HEM605 3.4 18.1 1.0
CHA A:HEM605 3.4 16.4 1.0
CHB A:HEM605 3.5 20.1 1.0
N8 A:SHA616 3.7 42.2 1.0
C3C A:HEM605 4.2 17.6 1.0
C2C A:HEM605 4.2 18.9 1.0
CG A:HIS351 4.3 19.6 1.0
NE2 A:GLN105 4.3 19.3 1.0
C2A A:HEM605 4.3 19.7 1.0
C3B A:HEM605 4.3 20.6 1.0
ND1 A:HIS351 4.3 15.5 1.0
C3A A:HEM605 4.3 24.6 1.0
C2B A:HEM605 4.3 23.6 1.0
C2D A:HEM605 4.3 15.8 1.0
C3D A:HEM605 4.3 15.9 1.0
C7 A:SHA616 4.7 33.4 1.0
CG A:GLN105 4.7 19.7 1.0
CD A:GLN105 4.8 18.6 1.0
CD2 A:LEU433 4.9 17.0 1.0

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 2017.
ISSN: ISSN 0006-3002
PubMed: 27986533
DOI: 10.1016/J.BBAPAP.2016.12.006
Page generated: Sun Aug 4 01:49:29 2024

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