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Iron in PDB 2iuf: The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole

Enzymatic activity of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole

All present enzymatic activity of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole:
1.11.1.6;

Protein crystallography data

The structure of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole, PDB code: 2iuf was solved by G.Murshudov, A.Borovik, A.Grebenko, V.Barynin, A.Vagin, W.Melik-Adamyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 119.52 / 1.71
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.440, 142.440, 132.230, 90.00, 90.00, 120.00
R / Rfree (%) 12.9 / 15.4

Other elements in 2iuf:

The structure of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole also contains other interesting chemical elements:

Calcium (Ca) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole (pdb code 2iuf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole, PDB code: 2iuf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2iuf

Go back to Iron Binding Sites List in 2iuf
Iron binding site 1 out of 2 in the The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1691

b:12.6
occ:1.00
FE A:HDD1691 0.0 12.6 1.0
O A:O1695 1.7 12.0 1.0
NC A:HDD1691 2.0 11.5 1.0
OH A:TYR351 2.0 12.1 1.0
NA A:HDD1691 2.0 11.0 1.0
NB A:HDD1691 2.0 11.2 1.0
ND A:HDD1691 2.1 10.5 1.0
CZ A:TYR351 3.0 10.0 1.0
C4B A:HDD1691 3.0 14.1 1.0
C1C A:HDD1691 3.0 12.7 1.0
C1A A:HDD1691 3.0 9.6 1.0
C4C A:HDD1691 3.0 11.6 1.0
C4A A:HDD1691 3.0 8.7 1.0
C1B A:HDD1691 3.1 12.6 1.0
C1D A:HDD1691 3.1 12.2 1.0
C4D A:HDD1691 3.1 10.4 1.0
CHC A:HDD1691 3.4 13.6 1.0
CHA A:HDD1691 3.4 10.4 1.0
CHD A:HDD1691 3.4 12.4 1.0
CHB A:HDD1691 3.5 9.8 1.0
CE2 A:TYR351 3.8 9.8 1.0
CE1 A:TYR351 3.9 14.0 1.0
NE A:ARG347 4.2 11.9 1.0
C3C A:HDD1691 4.2 13.5 1.0
C2A A:HDD1691 4.2 9.4 1.0
C2C A:HDD1691 4.2 11.2 1.0
C3B A:HDD1691 4.3 11.9 1.0
C3A A:HDD1691 4.3 10.5 1.0
NH2 A:ARG347 4.3 10.6 1.0
C2B A:HDD1691 4.3 12.4 1.0
O A:HOH2105 4.3 17.1 1.0
C2D A:HDD1691 4.4 9.8 1.0
C3D A:HDD1691 4.4 10.8 1.0
NE2 A:HIS64 4.4 11.6 1.0
CG2 A:VAL63 4.4 11.6 1.0
CZ A:PHE150 4.5 12.6 1.0
CD2 A:HIS64 4.5 12.1 1.0
CZ A:ARG347 4.6 12.4 1.0
CE2 A:PHE150 4.9 12.3 1.0

Iron binding site 2 out of 2 in 2iuf

Go back to Iron Binding Sites List in 2iuf
Iron binding site 2 out of 2 in the The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structures of Penicillium Vitale Catalase: Resting State, Oxidised State (Compound I) and Complex with Aminotriazole within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1691

b:13.2
occ:1.00
FE E:HDD1691 0.0 13.2 1.0
O E:O1696 1.7 12.2 1.0
NC E:HDD1691 2.0 11.1 1.0
NA E:HDD1691 2.0 10.2 1.0
NB E:HDD1691 2.0 9.8 1.0
OH E:TYR351 2.0 13.6 1.0
ND E:HDD1691 2.1 11.2 1.0
C1A E:HDD1691 3.0 9.8 1.0
C4B E:HDD1691 3.0 13.0 1.0
C4A E:HDD1691 3.0 10.6 1.0
C1B E:HDD1691 3.0 11.5 1.0
C1C E:HDD1691 3.0 14.8 1.0
C4C E:HDD1691 3.1 10.3 1.0
CZ E:TYR351 3.1 11.4 1.0
C1D E:HDD1691 3.1 13.9 1.0
C4D E:HDD1691 3.1 8.8 1.0
CHC E:HDD1691 3.4 14.0 1.0
CHA E:HDD1691 3.4 10.7 1.0
CHB E:HDD1691 3.4 11.3 1.0
CHD E:HDD1691 3.4 13.0 1.0
CE2 E:TYR351 3.8 11.2 1.0
CE1 E:TYR351 3.9 12.4 1.0
NE E:ARG347 4.2 12.0 1.0
NH2 E:ARG347 4.2 11.1 1.0
C3A E:HDD1691 4.2 12.3 1.0
C2A E:HDD1691 4.2 10.2 1.0
C3B E:HDD1691 4.2 16.0 1.0
C3C E:HDD1691 4.3 12.4 1.0
C2B E:HDD1691 4.3 13.1 1.0
C2C E:HDD1691 4.3 11.0 1.0
O E:HOH2090 4.3 18.5 1.0
C2D E:HDD1691 4.4 10.6 1.0
C3D E:HDD1691 4.4 10.9 1.0
CG2 E:VAL63 4.4 10.0 1.0
NE2 E:HIS64 4.4 12.4 1.0
CZ E:PHE150 4.5 13.1 1.0
CD2 E:HIS64 4.5 11.7 1.0
CZ E:ARG347 4.6 14.2 1.0
CE2 E:PHE150 5.0 12.7 1.0

Reference:

M.Alfonso-Prieto, A.Borovik, X.Carpena, G.Murshudov, W.Melik-Adamyan, I.Fita, C.Rovira, P.C.Loewen. The Structures and Electronic Configuration of Compound I Intermediates of Helicobacter Pylori and Penicillium Vitale Catalases Determined By X-Ray Crystallography and Qm/Mm Density Functional Theory Calculations. J.Am.Chem.Soc. V. 129 4193 2007.
ISSN: ISSN 0002-7863
PubMed: 17358056
DOI: 10.1021/JA063660Y
Page generated: Sun Dec 13 14:47:13 2020

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