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Iron in PDB 1sqd: Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases

Enzymatic activity of Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases

All present enzymatic activity of Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases:
1.13.11.27;

Protein crystallography data

The structure of Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases, PDB code: 1sqd was solved by C.Yang, J.W.Pflugrath, D.L.Camper, M.L.Foster, D.J.Pernich, T.A.Walsh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.400, 83.600, 63.500, 90.00, 102.50, 90.00
R / Rfree (%) 21.6 / 26.6

Iron Binding Sites:

The binding sites of Iron atom in the Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases (pdb code 1sqd). 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 Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases, PDB code: 1sqd:

Iron binding site 1 out of 1 in 1sqd

Go back to Iron Binding Sites List in 1sqd
Iron binding site 1 out of 1 in the Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structural Basis For Inhibitor Selectivity Revealed By Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:2.9
occ:1.00
 O A:HOH1012 1.9 15.5 1.0
NE2 A:HIS205 1.9 20.8 1.0
NE2 A:HIS287 2.1 20.0 1.0
OE2 A:GLU373 2.2 21.9 1.0
O A:HOH1011 2.4 25.8 1.0
O A:HOH1001 2.5 24.7 1.0
CE1 A:HIS205 2.9 14.7 1.0
CE1 A:HIS287 2.9 21.3 1.0
CD2 A:HIS205 2.9 17.9 1.0
CD2 A:HIS287 3.2 20.7 1.0
CD A:GLU373 3.3 25.5 1.0
OE1 A:GLU373 3.8 23.8 1.0
ND1 A:HIS205 4.0 18.8 1.0
CG A:HIS205 4.1 18.6 1.0
ND1 A:HIS287 4.1 18.8 1.0
CG A:HIS287 4.2 19.5 1.0
CB A:ALA289 4.3 20.4 1.0
CG2 A:VAL207 4.3 18.8 1.0
CG A:GLU373 4.6 21.1 1.0
CE2 A:PHE360 4.7 25.2 1.0
O A:PHE398 4.7 31.6 1.0
CB A:GLU373 4.7 18.2 1.0
CD2 A:PHE398 4.8 17.5 1.0
CZ A:PHE360 5.0 26.7 1.0

Reference:

C.Yang, J.W.Pflugrath, D.L.Camper, M.L.Foster, D.J.Pernich, T.A.Walsh. Structural Basis For Herbicidal Inhibitor Selectivity Revealed By Comparison of Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases Biochemistry V. 43 10414 2004.
ISSN: ISSN 0006-2960
PubMed: 15301540
DOI: 10.1021/BI049323O
Page generated: Sat Aug 3 14:49:33 2024

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