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Iron in PDB 1sp8: 4-Hydroxyphenylpyruvate Dioxygenase

Protein crystallography data

The structure of 4-Hydroxyphenylpyruvate Dioxygenase, PDB code: 1sp8 was solved by I.M.Fritze, L.Linden, J.Freigang, G.Auerbach, R.Huber, S.Steinbacher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.84 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 89.000, 110.900, 174.800, 90.00, 90.00, 90.00
R / Rfree (%) 27.5 / 32.4

Iron Binding Sites:

The binding sites of Iron atom in the 4-Hydroxyphenylpyruvate Dioxygenase (pdb code 1sp8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 4-Hydroxyphenylpyruvate Dioxygenase, PDB code: 1sp8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1sp8

Go back to Iron Binding Sites List in 1sp8
Iron binding site 1 out of 4 in the 4-Hydroxyphenylpyruvate Dioxygenase


Mono view


Stereo pair view

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

b:76.3
occ:1.00
OE1 A:GLU387 2.1 55.9 1.0
O A:HOH501 2.1 61.5 1.0
O A:HOH502 2.1 57.4 1.0
NE2 A:HIS219 2.1 52.7 1.0
NE2 A:HIS301 2.2 51.4 1.0
CE1 A:HIS301 3.0 29.7 1.0
CE1 A:HIS219 3.0 37.2 1.0
CD A:GLU387 3.2 40.4 1.0
CD2 A:HIS219 3.2 39.4 1.0
CD2 A:HIS301 3.3 32.8 1.0
OE2 A:GLU387 3.6 36.3 1.0
ND1 A:HIS219 4.2 39.8 1.0
ND1 A:HIS301 4.2 31.2 1.0
CG A:HIS219 4.3 40.3 1.0
CG A:HIS301 4.4 35.2 1.0
CG A:GLU387 4.5 35.3 1.0
CB A:ALA303 4.5 28.7 1.0
CG2 A:VAL221 4.5 37.9 1.0
CE1 A:PHE374 4.6 41.1 1.0
CB A:GLU387 4.7 33.4 1.0
CD1 A:PHE412 4.7 39.4 1.0
O A:HOH718 4.8 59.0 1.0
CZ A:PHE374 4.8 38.0 1.0
O A:PHE412 4.9 49.1 1.0

Iron binding site 2 out of 4 in 1sp8

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Iron binding site 2 out of 4 in the 4-Hydroxyphenylpyruvate Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 4-Hydroxyphenylpyruvate Dioxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:62.5
occ:1.00
O B:HOH501 2.1 51.5 1.0
O B:HOH502 2.1 56.0 1.0
OE1 B:GLU387 2.1 41.3 1.0
O B:HOH503 2.1 52.8 1.0
NE2 B:HIS219 2.1 40.0 1.0
NE2 B:HIS301 2.1 39.8 1.0
CE1 B:HIS301 2.9 35.1 1.0
CE1 B:HIS219 3.0 37.0 1.0
CD2 B:HIS219 3.2 36.9 1.0
CD B:GLU387 3.2 40.8 1.0
CD2 B:HIS301 3.3 36.5 1.0
OE2 B:GLU387 3.7 38.9 1.0
ND1 B:HIS301 4.1 35.5 1.0
ND1 B:HIS219 4.2 38.6 1.0
CG B:HIS219 4.3 35.6 1.0
CG B:HIS301 4.3 33.9 1.0
CB B:ALA303 4.4 26.5 1.0
CG2 B:VAL221 4.4 31.0 1.0
CE1 B:PHE374 4.4 40.4 1.0
CG B:GLU387 4.5 35.5 1.0
CB B:GLU387 4.6 35.0 1.0
CZ B:PHE374 4.7 37.2 1.0

Iron binding site 3 out of 4 in 1sp8

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Iron binding site 3 out of 4 in the 4-Hydroxyphenylpyruvate Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 4-Hydroxyphenylpyruvate Dioxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:40.8
occ:1.00
O C:HOH502 2.1 51.8 1.0
O C:HOH501 2.1 50.2 1.0
O C:HOH503 2.1 50.0 1.0
OE1 C:GLU387 2.1 47.2 1.0
NE2 C:HIS219 2.1 46.5 1.0
NE2 C:HIS301 2.2 44.4 1.0
CE1 C:HIS301 3.0 34.5 1.0
CE1 C:HIS219 3.0 41.9 1.0
CD C:GLU387 3.2 41.0 1.0
CD2 C:HIS219 3.2 40.8 1.0
CD2 C:HIS301 3.3 34.1 1.0
OE2 C:GLU387 3.6 43.2 1.0
ND1 C:HIS301 4.2 39.5 1.0
ND1 C:HIS219 4.2 44.0 1.0
CG C:HIS219 4.3 41.1 1.0
CG C:HIS301 4.3 37.8 1.0
CE1 C:PHE374 4.5 39.5 1.0
CG C:GLU387 4.5 37.4 1.0
CB C:ALA303 4.6 28.9 1.0
O C:HOH660 4.6 62.1 1.0
CG2 C:VAL221 4.7 35.8 1.0
CZ C:PHE374 4.7 41.4 1.0
CB C:GLU387 4.7 29.5 1.0
O C:PHE412 4.8 46.5 1.0

Iron binding site 4 out of 4 in 1sp8

Go back to Iron Binding Sites List in 1sp8
Iron binding site 4 out of 4 in the 4-Hydroxyphenylpyruvate Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 4-Hydroxyphenylpyruvate Dioxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:62.5
occ:1.00
OE1 D:GLU387 2.1 43.0 1.0
O D:HOH501 2.1 51.0 1.0
O D:HOH502 2.1 56.2 1.0
NE2 D:HIS219 2.1 39.8 1.0
O D:HOH503 2.1 53.2 1.0
NE2 D:HIS301 2.2 37.2 1.0
CE1 D:HIS301 3.0 29.2 1.0
CE1 D:HIS219 3.1 36.7 1.0
CD2 D:HIS219 3.1 33.0 1.0
CD D:GLU387 3.2 43.9 1.0
CD2 D:HIS301 3.2 32.7 1.0
OE2 D:GLU387 3.6 46.4 1.0
ND1 D:HIS301 4.2 31.1 1.0
ND1 D:HIS219 4.2 34.4 1.0
CG D:HIS219 4.3 33.7 1.0
CG D:HIS301 4.3 27.4 1.0
CE1 D:PHE374 4.4 40.8 1.0
CG2 D:VAL221 4.4 31.5 1.0
CG D:GLU387 4.5 38.7 1.0
CB D:ALA303 4.5 27.6 1.0
CB D:GLU387 4.7 35.5 1.0
CZ D:PHE374 4.8 38.1 1.0
CD1 D:PHE412 5.0 42.3 1.0
O D:PHE412 5.0 44.1 1.0

Reference:

I.M.Fritze, L.Linden, J.Freigang, G.Auerbach, R.Huber, S.Steinbacher. The Crystal Structures of Zea Mays and Arabidopsis 4-Hydroxyphenylpyruvate Dioxygenase Plant Physiol. V. 134 1388 2004.
ISSN: ISSN 0032-0889
PubMed: 15084729
DOI: 10.1104/PP.103.034082
Page generated: Sat Aug 3 14:47:48 2024

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