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Iron in PDB 5jhz: Crystal Structure of Fungal MAGKATG2 at pH 7.0

Enzymatic activity of Crystal Structure of Fungal MAGKATG2 at pH 7.0

All present enzymatic activity of Crystal Structure of Fungal MAGKATG2 at pH 7.0:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of Fungal MAGKATG2 at pH 7.0, PDB code: 5jhz was solved by B.Gasselhuber, C.Obinger, X.Carpena, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 103.200, 109.380, 133.370, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 18.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Fungal MAGKATG2 at pH 7.0 (pdb code 5jhz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Fungal MAGKATG2 at pH 7.0, PDB code: 5jhz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5jhz

Go back to Iron Binding Sites List in 5jhz
Iron binding site 1 out of 2 in the Crystal Structure of Fungal MAGKATG2 at pH 7.0


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 Fungal MAGKATG2 at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1500

b:14.4
occ:1.00
FE A:HEM1500 0.0 14.4 1.0
ND A:HEM1500 1.9 14.6 1.0
NA A:HEM1500 2.0 14.5 1.0
NC A:HEM1500 2.0 14.3 1.0
NB A:HEM1500 2.1 14.3 1.0
NE2 A:HIS314 2.2 14.7 1.0
O A:HOH1775 2.8 35.1 1.0
C4D A:HEM1500 3.0 14.7 1.0
C1D A:HEM1500 3.0 14.6 1.0
C1A A:HEM1500 3.0 14.5 1.0
C4C A:HEM1500 3.0 14.3 1.0
C1C A:HEM1500 3.0 14.0 1.0
C4B A:HEM1500 3.1 14.0 1.0
C4A A:HEM1500 3.1 14.5 1.0
C1B A:HEM1500 3.1 14.2 1.0
CD2 A:HIS314 3.1 14.9 1.0
CE1 A:HIS314 3.2 14.8 1.0
CHA A:HEM1500 3.4 14.7 1.0
CHD A:HEM1500 3.4 14.5 1.0
CHC A:HEM1500 3.4 14.0 1.0
CHB A:HEM1500 3.5 14.4 1.0
NE1 A:TRP140 4.2 13.9 1.0
C2C A:HEM1500 4.2 13.9 1.0
C2A A:HEM1500 4.2 14.6 1.0
C3C A:HEM1500 4.2 14.1 1.0
C2D A:HEM1500 4.2 14.9 1.0
C3D A:HEM1500 4.2 14.9 1.0
C3A A:HEM1500 4.2 14.5 1.0
C2B A:HEM1500 4.3 14.2 1.0
C3B A:HEM1500 4.3 14.1 1.0
ND1 A:HIS314 4.3 15.0 1.0
CG A:HIS314 4.3 15.0 1.0
O A:HOH2236 4.5 47.9 1.0
CD1 A:TRP140 4.5 14.0 1.0
CH2 A:TRP365 4.8 15.3 1.0

Iron binding site 2 out of 2 in 5jhz

Go back to Iron Binding Sites List in 5jhz
Iron binding site 2 out of 2 in the Crystal Structure of Fungal MAGKATG2 at pH 7.0


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Fungal MAGKATG2 at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1500

b:14.4
occ:1.00
FE B:HEM1500 0.0 14.4 1.0
ND B:HEM1500 2.0 14.2 1.0
NA B:HEM1500 2.0 14.6 1.0
NB B:HEM1500 2.1 14.4 1.0
NC B:HEM1500 2.1 14.0 1.0
NE2 B:HIS314 2.2 14.8 1.0
O B:HOH1740 2.8 35.6 1.0
C4D B:HEM1500 3.0 14.4 1.0
C1D B:HEM1500 3.0 14.1 1.0
C4B B:HEM1500 3.0 14.3 1.0
C1A B:HEM1500 3.0 14.6 1.0
C1B B:HEM1500 3.0 14.6 1.0
C4A B:HEM1500 3.0 14.7 1.0
C4C B:HEM1500 3.1 14.0 1.0
C1C B:HEM1500 3.1 14.0 1.0
CD2 B:HIS314 3.1 14.9 1.0
CE1 B:HIS314 3.2 15.0 1.0
CHA B:HEM1500 3.4 14.6 1.0
CHC B:HEM1500 3.4 14.0 1.0
CHD B:HEM1500 3.4 14.0 1.0
CHB B:HEM1500 3.4 14.6 1.0
NE1 B:TRP140 4.1 14.0 1.0
C3A B:HEM1500 4.2 14.8 1.0
C2A B:HEM1500 4.2 14.7 1.0
C2D B:HEM1500 4.2 14.2 1.0
C3D B:HEM1500 4.3 14.3 1.0
C3B B:HEM1500 4.3 14.5 1.0
C2B B:HEM1500 4.3 14.6 1.0
C3C B:HEM1500 4.3 13.8 1.0
ND1 B:HIS314 4.3 15.2 1.0
C2C B:HEM1500 4.3 13.8 1.0
CG B:HIS314 4.3 15.1 1.0
O B:HOH2295 4.5 50.3 1.0
CD1 B:TRP140 4.5 13.9 1.0
CH2 B:TRP365 4.9 15.4 1.0
CZ2 B:TRP365 5.0 15.5 1.0

Reference:

B.Gasselhuber, M.M.Graf, C.Jakopitsch, M.Zamocky, A.Nicolussi, P.G.Furtmuller, C.Oostenbrink, X.Carpena, C.Obinger. Interaction with the Redox Cofactor Myw and Functional Role of A Mobile Arginine in Eukaryotic Catalase-Peroxidase. Biochemistry V. 55 3528 2016.
ISSN: ISSN 0006-2960
PubMed: 27293030
DOI: 10.1021/ACS.BIOCHEM.6B00436
Page generated: Sun Dec 13 16:04:15 2020

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