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Iron in PDB 2ig9: Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.

Enzymatic activity of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.

All present enzymatic activity of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.:
1.13.11.15;

Protein crystallography data

The structure of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup., PDB code: 2ig9 was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.08 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.445, 152.802, 99.714, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 23.4

Other elements in 2ig9:

The structure of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. (pdb code 2ig9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup., PDB code: 2ig9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 2ig9

Go back to Iron Binding Sites List in 2ig9
Iron binding site 1 out of 4 in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:20.1
occ:1.00
 OE1 A:GLU267 2.0 16.9 1.0
O A:HOH810 2.1 21.2 1.0
O A:HOH809 2.2 19.7 1.0
O A:HOH808 2.3 17.2 1.0
NE2 A:HIS214 2.3 15.9 1.0
NE2 A:HIS155 2.4 20.6 1.0
CD A:GLU267 3.1 19.5 1.0
CE1 A:HIS214 3.2 16.3 1.0
CE1 A:HIS155 3.2 18.4 1.0
CD2 A:HIS214 3.3 17.3 1.0
CD2 A:HIS155 3.4 17.9 1.0
OE2 A:GLU267 3.6 18.6 1.0
NE2 A:HIS200 3.9 21.4 1.0
OH A:TYR257 4.1 16.6 1.0
ND1 A:HIS214 4.3 17.0 1.0
ND2 A:ASN157 4.3 16.1 1.0
ND1 A:HIS155 4.4 17.8 1.0
CG A:HIS214 4.4 16.6 1.0
O A:HOH977 4.4 31.1 1.0
CG A:GLU267 4.4 17.5 1.0
CE1 A:HIS200 4.5 21.0 1.0
CG A:HIS155 4.5 17.9 1.0
CB A:GLU267 4.5 17.3 1.0
CE1 A:TYR257 4.6 14.2 1.0
CB A:ALA216 4.6 16.4 1.0
CB A:ASN157 4.7 18.0 1.0
CZ A:TYR257 4.8 17.4 1.0
CD1 A:TYR269 5.0 22.8 1.0
CD2 A:HIS200 5.0 21.3 1.0

Iron binding site 2 out of 4 in 2ig9

Go back to Iron Binding Sites List in 2ig9
Iron binding site 2 out of 4 in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:18.1
occ:1.00
 OE1 B:GLU267 2.0 16.9 1.0
O B:HOH810 2.1 17.7 1.0
O B:HOH812 2.2 13.9 1.0
NE2 B:HIS155 2.2 14.5 1.0
NE2 B:HIS214 2.2 10.9 1.0
O B:HOH811 2.3 20.7 1.0
CE1 B:HIS214 3.1 9.4 1.0
CD B:GLU267 3.2 16.8 1.0
CE1 B:HIS155 3.2 12.2 1.0
CD2 B:HIS155 3.2 13.9 1.0
CD2 B:HIS214 3.3 13.1 1.0
OE2 B:GLU267 3.7 17.8 1.0
NE2 B:HIS200 3.8 20.8 1.0
OH B:TYR257 4.1 16.6 1.0
ND1 B:HIS214 4.2 13.1 1.0
ND2 B:ASN157 4.2 14.4 1.0
ND1 B:HIS155 4.3 16.5 1.0
CG B:HIS155 4.3 14.7 1.0
CG B:HIS214 4.4 14.5 1.0
CG B:GLU267 4.4 14.1 1.0
CE1 B:HIS200 4.5 19.2 1.0
O B:HOH948 4.5 26.2 1.0
CB B:GLU267 4.5 15.6 1.0
CB B:ASN157 4.6 15.0 1.0
CE1 B:TYR257 4.6 13.4 1.0
CB B:ALA216 4.7 15.1 1.0
CZ B:TYR257 4.8 17.3 1.0
CD2 B:HIS200 4.8 19.0 1.0
CG B:ASN157 4.9 17.1 1.0

Iron binding site 3 out of 4 in 2ig9

Go back to Iron Binding Sites List in 2ig9
Iron binding site 3 out of 4 in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:21.1
occ:1.00
 OE1 C:GLU267 2.0 19.1 1.0
O C:HOH809 2.1 19.5 1.0
O C:HOH811 2.1 18.3 1.0
O C:HOH810 2.2 18.1 1.0
NE2 C:HIS214 2.2 16.6 1.0
NE2 C:HIS155 2.3 20.2 1.0
CE1 C:HIS214 3.0 16.9 1.0
CD C:GLU267 3.1 20.8 1.0
CE1 C:HIS155 3.1 20.7 1.0
CD2 C:HIS155 3.3 17.5 1.0
CD2 C:HIS214 3.3 16.4 1.0
OE2 C:GLU267 3.5 25.2 1.0
NE2 C:HIS200 3.8 24.4 1.0
OH C:TYR257 4.1 17.9 1.0
ND1 C:HIS214 4.2 16.4 1.0
ND1 C:HIS155 4.3 20.1 1.0
CG C:GLU267 4.3 17.8 1.0
O C:HOH850 4.3 28.1 1.0
CG C:HIS214 4.3 17.8 1.0
CG C:HIS155 4.4 18.2 1.0
CE1 C:HIS200 4.5 21.6 1.0
CE1 C:TYR257 4.5 16.7 1.0
CB C:GLU267 4.5 18.0 1.0
ND2 C:ASN157 4.5 23.1 1.0
CB C:ALA216 4.6 18.8 1.0
CB C:ASN157 4.7 22.0 1.0
CZ C:TYR257 4.8 17.9 1.0
CD1 C:TYR269 4.9 24.4 1.0
CD2 C:HIS200 4.9 24.1 1.0
CE1 C:TYR269 5.0 22.0 1.0
NE2 C:HIS248 5.0 19.8 1.0

Iron binding site 4 out of 4 in 2ig9

Go back to Iron Binding Sites List in 2ig9
Iron binding site 4 out of 4 in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:19.6
occ:1.00
 OE1 D:GLU267 2.0 19.1 1.0
O D:HOH814 2.1 18.0 1.0
NE2 D:HIS155 2.2 18.6 1.0
O D:HOH813 2.2 16.0 1.0
NE2 D:HIS214 2.2 12.5 1.0
O D:HOH812 2.3 20.4 1.0
CD D:GLU267 3.1 18.2 1.0
CE1 D:HIS155 3.1 20.1 1.0
CE1 D:HIS214 3.1 12.3 1.0
CD2 D:HIS155 3.3 19.1 1.0
CD2 D:HIS214 3.3 14.6 1.0
OE2 D:GLU267 3.5 19.5 1.0
NE2 D:HIS200 3.9 23.6 1.0
OH D:TYR257 4.1 15.8 1.0
ND1 D:HIS155 4.2 18.1 1.0
ND1 D:HIS214 4.3 10.9 1.0
ND2 D:ASN157 4.3 20.7 1.0
CG D:HIS155 4.4 19.0 1.0
CG D:HIS214 4.4 14.2 1.0
CG D:GLU267 4.4 16.6 1.0
O D:HOH855 4.4 22.2 1.0
CE1 D:TYR257 4.5 14.8 1.0
CB D:GLU267 4.6 17.7 1.0
CB D:ALA216 4.6 14.5 1.0
CB D:ASN157 4.7 19.1 1.0
CE1 D:HIS200 4.7 21.2 1.0
CZ D:TYR257 4.8 15.6 1.0
CD1 D:TYR269 4.9 18.6 1.0
CD2 D:HIS200 4.9 20.3 1.0
CG D:ASN157 5.0 21.4 1.0
CE1 D:TYR269 5.0 19.9 1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Crystal Structures of FE2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates Science V. 316 453 2007.
ISSN: ISSN 0036-8075
PubMed: 17446402
DOI: 10.1126/SCIENCE.1134697
Page generated: Thu Jul 17 02:15:39 2025

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