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Iron in PDB 3x16: Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942

Enzymatic activity of Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942, PDB code: 3x16 was solved by T.Tada, K.Wada, S.Kamachi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.33 / 2.65
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.254, 108.254, 203.225, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 25.4

Other elements in 3x16:

The structure of Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942 also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942 (pdb code 3x16). 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 Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942, PDB code: 3x16:

Iron binding site 1 out of 1 in 3x16

Go back to Iron Binding Sites List in 3x16
Iron binding site 1 out of 1 in the Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942


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 Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:37.3
occ:1.00
 FE A:HEB801 0.0 37.3 1.0
NE2 A:HIS263 2.0 35.9 1.0
NB A:HEB801 2.0 33.9 1.0
NC A:HEB801 2.1 35.5 1.0
NA A:HEB801 2.1 38.7 1.0
ND A:HEB801 2.1 31.3 1.0
CE1 A:HIS263 2.9 38.1 1.0
C1A A:HEB801 3.0 33.7 1.0
C1C A:HEB801 3.0 37.3 1.0
C1D A:HEB801 3.0 30.6 1.0
C4C A:HEB801 3.0 33.2 1.0
CD2 A:HIS263 3.0 35.1 1.0
C4B A:HEB801 3.0 35.3 1.0
C1B A:HEB801 3.1 37.0 1.0
C4A A:HEB801 3.1 37.5 1.0
C4D A:HEB801 3.1 31.4 1.0
CHD A:HEB801 3.4 33.2 1.0
CHA A:HEB801 3.4 35.2 1.0
CHC A:HEB801 3.4 35.3 1.0
CHB A:HEB801 3.5 34.5 1.0
O A:HOH1038 4.0 54.6 1.0
O A:HOH958 4.0 47.2 1.0
ND1 A:HIS263 4.1 31.2 1.0
CG A:HIS263 4.2 33.2 1.0
NE1 A:TRP94 4.3 43.7 1.0
C2A A:HEB801 4.3 34.3 1.0
C3C A:HEB801 4.3 35.7 1.0
C2D A:HEB801 4.4 32.0 1.0
C2C A:HEB801 4.4 36.1 1.0
C3A A:HEB801 4.4 32.8 1.0
C3B A:HEB801 4.4 34.5 1.0
C2B A:HEB801 4.4 38.9 1.0
C3D A:HEB801 4.4 29.8 1.0
CD1 A:TRP94 4.5 41.7 1.0
CH2 A:TRP314 4.8 38.6 1.0
CZ2 A:TRP314 4.9 35.3 1.0

Reference:

S.Kamachi, K.Hirabayashi, M.Tamoi, S.Shigeoka, T.Tada, K.Wada. Crystal Structure of the Catalase-Peroxidase Katg W78F Mutant From Synechococcus Elongatus PCC7942 in Complex with the Antitubercular Pro-Drug Isoniazid. Febs Lett. 2014.
ISSN: ISSN 0014-5793
PubMed: 25479089
DOI: 10.1016/J.FEBSLET.2014.11.037
Page generated: Sun Aug 4 22:54:32 2024

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