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Iron in PDB 1tg5: Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645

Enzymatic activity of Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645

All present enzymatic activity of Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645:
1.13.11.27;

Protein crystallography data

The structure of Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645, PDB code: 1tg5 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 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.464, 83.871, 63.301, 90.00, 102.28, 90.00
R / Rfree (%) 18.8 / 23.4

Other elements in 1tg5:

The structure of Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645 also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645 (pdb code 1tg5). 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 Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645, PDB code: 1tg5:

Iron binding site 1 out of 1 in 1tg5

Go back to Iron Binding Sites List in 1tg5
Iron binding site 1 out of 1 in the Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of Plant 4-Hydroxyphenylpyruvate Dioxygenases Complexed with DAS645 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:12.1
occ:1.00
 NE2 A:HIS205 2.0 14.7 1.0
O1 A:645501 2.2 16.7 1.0
O2 A:645501 2.2 10.1 1.0
NE2 A:HIS287 2.2 17.1 1.0
OE1 A:GLU373 2.3 14.8 1.0
O A:HOH1001 2.6 24.9 1.0
CD2 A:HIS205 2.9 14.8 1.0
CE1 A:HIS205 3.0 14.7 1.0
C1 A:645501 3.1 19.5 1.0
CE1 A:HIS287 3.2 17.1 1.0
CD2 A:HIS287 3.2 17.1 1.0
CD A:GLU373 3.4 14.8 1.0
C3 A:645501 3.5 15.3 1.0
C2 A:645501 3.5 18.4 1.0
OE2 A:GLU373 3.8 14.8 1.0
ND1 A:HIS205 4.1 14.7 1.0
CG A:HIS205 4.1 14.8 1.0
CB A:ALA289 4.3 15.6 1.0
ND1 A:HIS287 4.3 17.1 1.0
CG A:HIS287 4.4 17.0 1.0
N2 A:645501 4.4 21.0 1.0
CG2 A:VAL207 4.5 15.2 1.0
CD2 A:PHE398 4.6 24.0 1.0
C14 A:645501 4.6 22.1 1.0
C4 A:645501 4.6 20.6 1.0
CG A:GLU373 4.7 14.8 1.0
O A:PHE398 4.7 26.8 1.0
CB A:GLU373 4.8 14.7 1.0
CB A:PHE398 4.9 25.1 1.0
CE2 A:PHE360 4.9 20.1 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: Sun Dec 13 14:32:36 2020

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