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Iron in PDB 2nox: Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans

Enzymatic activity of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans

All present enzymatic activity of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans:
1.13.11.11;

Protein crystallography data

The structure of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans, PDB code: 2nox was solved by Y.Zhang, S.A.Kang, T.Mukherjee, S.Bale, B.R.Crane, T.P.Begley, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.12 / 2.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 72.544, 132.121, 139.950, 66.97, 85.06, 89.89
R / Rfree (%) 21 / 27

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans (pdb code 2nox). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 16 binding sites of Iron where determined in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans, PDB code: 2nox:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 16 in 2nox

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Iron binding site 1 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:30.1
occ:1.00
FE A:HEM500 0.0 30.1 1.0
NA A:HEM500 2.0 30.1 1.0
ND A:HEM500 2.1 30.5 1.0
NC A:HEM500 2.1 21.3 1.0
NE2 A:HIS257 2.1 26.7 1.0
O A:HOH614 2.2 32.8 1.0
NB A:HEM500 2.2 26.1 1.0
CE1 A:HIS257 2.9 34.0 1.0
C4A A:HEM500 3.0 37.6 1.0
C1A A:HEM500 3.0 37.2 1.0
C4D A:HEM500 3.1 22.5 1.0
C1D A:HEM500 3.1 18.9 1.0
C4C A:HEM500 3.1 27.9 1.0
C1B A:HEM500 3.1 29.0 1.0
C1C A:HEM500 3.2 32.5 1.0
C4B A:HEM500 3.2 30.5 1.0
CD2 A:HIS257 3.3 31.2 1.0
CHA A:HEM500 3.4 33.6 1.0
CHB A:HEM500 3.4 30.5 1.0
CHD A:HEM500 3.4 27.6 1.0
CHC A:HEM500 3.6 25.9 1.0
ND1 A:HIS257 4.1 34.1 1.0
C2A A:HEM500 4.2 32.4 1.0
C3A A:HEM500 4.2 23.0 1.0
CG A:HIS257 4.3 33.0 1.0
C2D A:HEM500 4.3 25.7 1.0
C3D A:HEM500 4.3 35.0 1.0
C3C A:HEM500 4.3 22.0 1.0
C2C A:HEM500 4.4 29.9 1.0
C2B A:HEM500 4.4 38.5 1.0
C3B A:HEM500 4.4 39.7 1.0
CG2 A:VAL261 4.4 35.9 1.0
NE2 A:HIS72 4.8 35.7 1.0
N A:GLY142 4.8 48.5 1.0
CA A:GLY142 4.9 46.5 1.0

Iron binding site 2 out of 16 in 2nox

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Iron binding site 2 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:41.2
occ:1.00
FE B:HEM500 0.0 41.2 1.0
NA B:HEM500 2.0 44.2 1.0
NB B:HEM500 2.1 46.7 1.0
ND B:HEM500 2.2 44.9 1.0
NC B:HEM500 2.2 39.7 1.0
NE2 B:HIS257 2.2 35.2 1.0
CE1 B:HIS257 2.9 37.0 1.0
C4A B:HEM500 3.0 43.9 1.0
C1A B:HEM500 3.0 41.9 1.0
C1B B:HEM500 3.1 46.0 1.0
C4B B:HEM500 3.1 43.4 1.0
C4D B:HEM500 3.1 45.1 1.0
C1C B:HEM500 3.2 35.5 1.0
C4C B:HEM500 3.2 38.8 1.0
C1D B:HEM500 3.2 36.0 1.0
CHB B:HEM500 3.4 49.9 1.0
CHA B:HEM500 3.4 37.7 1.0
CD2 B:HIS257 3.4 37.4 1.0
CHC B:HEM500 3.5 46.7 1.0
CHD B:HEM500 3.6 33.0 1.0
ND1 B:HIS257 4.1 44.4 1.0
C3A B:HEM500 4.2 35.6 1.0
C2A B:HEM500 4.2 47.6 1.0
C2B B:HEM500 4.3 54.2 1.0
C3B B:HEM500 4.3 48.6 1.0
C3D B:HEM500 4.4 37.2 1.0
CG B:HIS257 4.4 43.7 1.0
C2C B:HEM500 4.4 35.5 1.0
C3C B:HEM500 4.4 36.5 1.0
C2D B:HEM500 4.4 41.9 1.0
CG2 B:VAL261 4.5 39.3 1.0
CD1 B:LEU280 5.0 34.6 1.0

Iron binding site 3 out of 16 in 2nox

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Iron binding site 3 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:45.4
occ:1.00
FE C:HEM500 0.0 45.4 1.0
NB C:HEM500 2.0 36.6 1.0
NC C:HEM500 2.1 39.4 1.0
ND C:HEM500 2.1 36.2 1.0
NA C:HEM500 2.1 45.5 1.0
NE2 C:HIS257 2.2 34.6 1.0
CE1 C:HIS257 2.9 37.0 1.0
C4B C:HEM500 3.1 46.5 1.0
C1B C:HEM500 3.1 46.6 1.0
C1C C:HEM500 3.1 35.9 1.0
C4A C:HEM500 3.1 43.7 1.0
C1D C:HEM500 3.1 33.9 1.0
C4C C:HEM500 3.1 33.4 1.0
C1A C:HEM500 3.1 51.9 1.0
C4D C:HEM500 3.1 41.6 1.0
CD2 C:HIS257 3.4 38.0 1.0
CHC C:HEM500 3.4 40.6 1.0
CHB C:HEM500 3.4 48.8 1.0
O C:HOH596 3.5 51.2 1.0
CHD C:HEM500 3.5 40.4 1.0
CHA C:HEM500 3.5 47.6 1.0
ND1 C:HIS257 4.1 36.7 1.0
C3B C:HEM500 4.3 52.3 1.0
C2B C:HEM500 4.3 47.7 1.0
C2C C:HEM500 4.3 32.3 1.0
C3A C:HEM500 4.3 51.8 1.0
C3C C:HEM500 4.3 32.9 1.0
C2A C:HEM500 4.3 56.5 1.0
C2D C:HEM500 4.3 28.5 1.0
CG C:HIS257 4.4 33.8 1.0
C3D C:HEM500 4.4 39.7 1.0
CG2 C:VAL261 4.4 40.6 1.0
CD1 C:LEU280 5.0 40.4 1.0
CA C:GLY142 5.0 50.1 1.0

Iron binding site 4 out of 16 in 2nox

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Iron binding site 4 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:30.3
occ:1.00
FE D:HEM500 0.0 30.3 1.0
NA D:HEM500 2.0 24.6 1.0
NC D:HEM500 2.1 23.1 1.0
ND D:HEM500 2.1 29.5 1.0
NB D:HEM500 2.2 27.2 1.0
NE2 D:HIS257 2.2 31.3 1.0
O D:HOH585 2.9 32.8 1.0
CE1 D:HIS257 3.0 39.2 1.0
C1A D:HEM500 3.1 37.0 1.0
C4A D:HEM500 3.1 30.1 1.0
C1C D:HEM500 3.1 32.1 1.0
C1D D:HEM500 3.1 28.7 1.0
C4C D:HEM500 3.1 32.8 1.0
C4D D:HEM500 3.1 33.4 1.0
C1B D:HEM500 3.2 32.4 1.0
C4B D:HEM500 3.2 29.8 1.0
CD2 D:HIS257 3.3 32.8 1.0
CHA D:HEM500 3.5 20.2 1.0
CHB D:HEM500 3.5 18.2 1.0
CHC D:HEM500 3.5 19.0 1.0
CHD D:HEM500 3.5 24.5 1.0
ND1 D:HIS257 4.2 29.1 1.0
C3A D:HEM500 4.2 32.5 1.0
C2A D:HEM500 4.2 28.8 1.0
C2C D:HEM500 4.3 32.0 1.0
C3C D:HEM500 4.3 30.0 1.0
C2D D:HEM500 4.3 38.7 1.0
C3D D:HEM500 4.4 32.0 1.0
CG D:HIS257 4.4 26.4 1.0
C2B D:HEM500 4.4 23.8 1.0
C3B D:HEM500 4.4 26.9 1.0
CG2 D:VAL261 4.5 35.1 1.0

Iron binding site 5 out of 16 in 2nox

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Iron binding site 5 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe500

b:35.2
occ:1.00
FE E:HEM500 0.0 35.2 1.0
NC E:HEM500 2.0 30.1 1.0
NB E:HEM500 2.0 31.7 1.0
NA E:HEM500 2.1 29.9 1.0
ND E:HEM500 2.1 33.3 1.0
NE2 E:HIS257 2.2 27.0 1.0
CE1 E:HIS257 2.9 27.1 1.0
C1D E:HEM500 3.0 32.1 1.0
C4A E:HEM500 3.0 39.3 1.0
C4C E:HEM500 3.0 27.1 1.0
C1B E:HEM500 3.1 29.9 1.0
O E:HOH575 3.1 56.0 1.0
C1C E:HEM500 3.1 30.9 1.0
C4B E:HEM500 3.1 28.1 1.0
C4D E:HEM500 3.1 38.1 1.0
C1A E:HEM500 3.1 38.2 1.0
CD2 E:HIS257 3.3 31.8 1.0
CHD E:HEM500 3.4 25.8 1.0
CHB E:HEM500 3.4 21.9 1.0
CHC E:HEM500 3.5 26.2 1.0
CHA E:HEM500 3.5 38.5 1.0
ND1 E:HIS257 4.1 36.3 1.0
C3A E:HEM500 4.3 32.5 1.0
C2D E:HEM500 4.3 38.1 1.0
C2C E:HEM500 4.3 30.2 1.0
C3C E:HEM500 4.3 33.2 1.0
C3B E:HEM500 4.3 32.0 1.0
C2B E:HEM500 4.3 37.4 1.0
C3D E:HEM500 4.3 33.7 1.0
CG E:HIS257 4.3 36.1 1.0
C2A E:HEM500 4.3 34.8 1.0
CG2 E:VAL261 4.4 34.1 1.0
O E:HOH554 4.8 32.9 1.0

Iron binding site 6 out of 16 in 2nox

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Iron binding site 6 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe500

b:47.6
occ:1.00
FE F:HEM500 0.0 47.6 1.0
ND F:HEM500 2.0 42.5 1.0
NC F:HEM500 2.0 41.8 1.0
NA F:HEM500 2.1 47.3 1.0
NB F:HEM500 2.1 48.7 1.0
NE2 F:HIS257 2.3 41.9 1.0
CE1 F:HIS257 2.9 42.8 1.0
C4D F:HEM500 3.0 51.5 1.0
C1A F:HEM500 3.0 47.5 1.0
C1D F:HEM500 3.0 45.6 1.0
C1C F:HEM500 3.1 46.1 1.0
C4C F:HEM500 3.1 42.4 1.0
C4B F:HEM500 3.1 45.0 1.0
C4A F:HEM500 3.1 43.2 1.0
C1B F:HEM500 3.1 42.9 1.0
CHA F:HEM500 3.4 49.8 1.0
CHD F:HEM500 3.4 46.6 1.0
CHC F:HEM500 3.4 40.7 1.0
CHB F:HEM500 3.5 41.9 1.0
CD2 F:HIS257 3.5 36.5 1.0
O F:HOH568 3.9 49.5 1.0
ND1 F:HIS257 4.2 44.9 1.0
O F:HOH566 4.2 51.1 1.0
C3D F:HEM500 4.2 53.4 1.0
C2D F:HEM500 4.3 39.9 1.0
C2C F:HEM500 4.3 49.1 1.0
C3C F:HEM500 4.3 42.2 1.0
C2A F:HEM500 4.3 49.4 1.0
C3A F:HEM500 4.3 51.7 1.0
C3B F:HEM500 4.3 46.2 1.0
C2B F:HEM500 4.4 49.8 1.0
CG F:HIS257 4.5 45.0 1.0
CG2 F:VAL261 4.5 41.4 1.0

Iron binding site 7 out of 16 in 2nox

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Iron binding site 7 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe500

b:48.5
occ:1.00
FE G:HEM500 0.0 48.5 1.0
NE2 G:HIS257 2.1 34.5 1.0
NC G:HEM500 2.1 53.4 1.0
NB G:HEM500 2.1 56.1 1.0
NA G:HEM500 2.1 56.7 1.0
ND G:HEM500 2.2 53.9 1.0
CE1 G:HIS257 2.7 36.9 1.0
C4C G:HEM500 3.1 43.9 1.0
C1C G:HEM500 3.1 54.2 1.0
C4A G:HEM500 3.1 52.8 1.0
C1B G:HEM500 3.1 57.9 1.0
C1D G:HEM500 3.1 59.2 1.0
C1A G:HEM500 3.1 53.0 1.0
C4D G:HEM500 3.2 52.0 1.0
C4B G:HEM500 3.2 51.0 1.0
CD2 G:HIS257 3.3 38.7 1.0
CHD G:HEM500 3.5 50.6 1.0
CHB G:HEM500 3.5 51.5 1.0
CHA G:HEM500 3.5 49.1 1.0
CHC G:HEM500 3.5 48.2 1.0
ND1 G:HIS257 3.9 37.5 1.0
CG G:HIS257 4.2 37.9 1.0
C2C G:HEM500 4.3 49.8 1.0
C3A G:HEM500 4.3 56.5 1.0
C3C G:HEM500 4.3 52.5 1.0
C2A G:HEM500 4.3 61.0 1.0
C2B G:HEM500 4.4 52.9 1.0
C3B G:HEM500 4.4 52.7 1.0
C2D G:HEM500 4.4 55.0 1.0
C3D G:HEM500 4.4 52.3 1.0
CG2 G:VAL261 4.4 40.6 1.0
CD1 G:LEU280 4.8 36.6 1.0

Iron binding site 8 out of 16 in 2nox

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Iron binding site 8 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe500

b:29.4
occ:1.00
FE H:HEM500 0.0 29.4 1.0
NB H:HEM500 2.0 28.8 1.0
NC H:HEM500 2.1 26.9 1.0
NA H:HEM500 2.1 16.9 1.0
ND H:HEM500 2.2 22.2 1.0
NE2 H:HIS257 2.3 27.1 1.0
C4B H:HEM500 3.0 32.6 1.0
C1C H:HEM500 3.0 34.1 1.0
CE1 H:HIS257 3.1 31.4 1.0
C1A H:HEM500 3.1 36.8 1.0
C4A H:HEM500 3.1 26.9 1.0
C1B H:HEM500 3.1 30.0 1.0
C4D H:HEM500 3.2 26.5 1.0
C4C H:HEM500 3.2 36.5 1.0
C1D H:HEM500 3.2 25.4 1.0
O H:HOH548 3.3 34.9 1.0
CHC H:HEM500 3.4 33.3 1.0
CD2 H:HIS257 3.4 24.0 1.0
CHA H:HEM500 3.5 30.8 1.0
CHB H:HEM500 3.5 21.3 1.0
CHD H:HEM500 3.6 31.0 1.0
OG H:SER141 4.2 56.2 0.5
ND1 H:HIS257 4.3 29.1 1.0
C3B H:HEM500 4.3 27.7 1.0
C3A H:HEM500 4.3 33.1 1.0
C2C H:HEM500 4.3 32.5 1.0
C2A H:HEM500 4.3 27.5 1.0
C2B H:HEM500 4.3 35.4 1.0
CG2 H:VAL261 4.3 27.4 1.0
C3C H:HEM500 4.4 29.0 1.0
C3D H:HEM500 4.4 28.1 1.0
CG H:HIS257 4.4 32.0 1.0
C2D H:HEM500 4.4 29.9 1.0
NE2 H:HIS72 5.0 34.6 1.0
CD1 H:LEU280 5.0 25.1 1.0

Iron binding site 9 out of 16 in 2nox

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Iron binding site 9 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe500

b:43.5
occ:1.00
FE I:HEM500 0.0 43.5 1.0
NC I:HEM500 2.0 37.6 1.0
NA I:HEM500 2.0 33.6 1.0
NB I:HEM500 2.0 32.2 1.0
ND I:HEM500 2.1 31.3 1.0
NE2 I:HIS257 2.2 33.8 1.0
C1C I:HEM500 3.0 34.7 1.0
CE1 I:HIS257 3.0 38.4 1.0
C4A I:HEM500 3.1 35.3 1.0
C1A I:HEM500 3.1 39.0 1.0
C4B I:HEM500 3.1 35.2 1.0
C1B I:HEM500 3.1 43.6 1.0
C4C I:HEM500 3.1 37.6 1.0
C1D I:HEM500 3.1 34.0 1.0
C4D I:HEM500 3.1 36.0 1.0
CD2 I:HIS257 3.3 35.6 1.0
CHC I:HEM500 3.4 33.5 1.0
CHA I:HEM500 3.4 40.5 1.0
CHB I:HEM500 3.5 40.7 1.0
CHD I:HEM500 3.5 27.4 1.0
ND1 I:HIS257 4.2 31.6 1.0
C2C I:HEM500 4.2 43.9 1.0
C3A I:HEM500 4.3 36.5 1.0
C2A I:HEM500 4.3 33.2 1.0
C3C I:HEM500 4.3 27.9 1.0
C3B I:HEM500 4.3 46.5 1.0
C2D I:HEM500 4.3 31.8 1.0
C3D I:HEM500 4.3 32.9 1.0
C2B I:HEM500 4.3 42.1 1.0
CG I:HIS257 4.4 42.1 1.0
CG2 I:VAL261 4.6 40.3 1.0
N I:GLY142 4.7 58.2 1.0
NE2 I:HIS72 4.8 31.1 1.0

Iron binding site 10 out of 16 in 2nox

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Iron binding site 10 out of 16 in the Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of Tryptophan 2,3-Dioxygenase From Ralstonia Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Fe500

b:48.7
occ:1.00
FE J:HEM500 0.0 48.7 1.0
NB J:HEM500 2.0 31.8 1.0
NA J:HEM500 2.0 47.9 1.0
ND J:HEM500 2.1 37.9 1.0
NC J:HEM500 2.1 32.1 1.0
NE2 J:HIS257 2.1 36.0 1.0
CE1 J:HIS257 2.7 38.3 1.0
C4A J:HEM500 3.0 42.9 1.0
C1B J:HEM500 3.0 40.9 1.0
C1A J:HEM500 3.1 38.4 1.0
C4B J:HEM500 3.1 33.0 1.0
C4D J:HEM500 3.1 46.0 1.0
C1D J:HEM500 3.1 49.6 1.0
C1C J:HEM500 3.1 31.9 1.0
C4C J:HEM500 3.1 41.0 1.0
CD2 J:HIS257 3.3 38.6 1.0
CHB J:HEM500 3.4 27.6 1.0
CHA J:HEM500 3.4 46.9 1.0
CHC J:HEM500 3.5 36.6 1.0
CHD J:HEM500 3.5 43.0 1.0
ND1 J:HIS257 4.0 36.1 1.0
C3A J:HEM500 4.2 42.5 1.0
C2A J:HEM500 4.3 44.8 1.0
C2B J:HEM500 4.3 42.8 1.0
CG J:HIS257 4.3 36.8 1.0
C3B J:HEM500 4.3 45.2 1.0
C2C J:HEM500 4.3 33.9 1.0
C2D J:HEM500 4.3 38.2 1.0
C3D J:HEM500 4.3 45.0 1.0
C3C J:HEM500 4.3 37.0 1.0
CG2 J:VAL261 4.5 38.9 1.0
CD1 J:LEU280 4.9 35.3 1.0

Reference:

Y.Zhang, S.A.Kang, T.Mukherjee, S.Bale, B.R.Crane, T.P.Begley, S.E.Ealick. Crystal Structure and Mechanism of Tryptophan 2,3-Dioxygenase, A Heme Enzyme Involved in Tryptophan Catabolism and in Quinolinate Biosynthesis. Biochemistry V. 46 145 2007.
ISSN: ISSN 0006-2960
PubMed: 17198384
DOI: 10.1021/BI0620095
Page generated: Sun Dec 13 14:49:49 2020

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