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Iron in PDB 3nw4: Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate

Enzymatic activity of Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate

All present enzymatic activity of Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate:
1.13.11.4;

Protein crystallography data

The structure of Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate, PDB code: 3nw4 was solved by M.Ferraroni, F.Briganti, I.Matera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.500, 86.890, 166.830, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 20.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate (pdb code 3nw4). 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 Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate, PDB code: 3nw4:

Iron binding site 1 out of 1 in 3nw4

Go back to Iron Binding Sites List in 3nw4
Iron binding site 1 out of 1 in the Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate


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 Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Gentisate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe369

b:23.9
occ:1.00
 OAD A:GTQ370 1.9 22.9 1.0
OAA A:GTQ370 2.0 25.3 1.0
NE2 A:HIS160 2.1 22.3 1.0
NE2 A:HIS119 2.2 28.3 1.0
NE2 A:HIS121 2.2 24.6 1.0
O A:HOH756 2.4 36.1 1.0
CAJ A:GTQ370 3.0 24.1 1.0
CE1 A:HIS160 3.0 22.5 1.0
CAH A:GTQ370 3.1 26.6 1.0
CE1 A:HIS121 3.2 23.7 1.0
CE1 A:HIS119 3.2 27.0 1.0
CD2 A:HIS160 3.2 25.7 1.0
CD2 A:HIS119 3.2 23.7 1.0
CD2 A:HIS121 3.3 26.6 1.0
CAK A:GTQ370 3.4 23.8 1.0
O A:HOH498 4.0 46.9 1.0
NH2 A:ARG127 4.0 16.5 0.5
ND1 A:HIS160 4.2 25.5 1.0
CAF A:GTQ370 4.2 24.3 1.0
OAB A:GTQ370 4.2 25.8 1.0
CG A:HIS160 4.3 24.2 1.0
ND1 A:HIS121 4.3 25.2 1.0
ND1 A:HIS119 4.3 25.0 1.0
CG A:HIS119 4.4 25.8 1.0
CG A:HIS121 4.4 23.8 1.0
NE A:ARG83 4.5 29.8 1.0
NH2 A:ARG83 4.5 29.7 1.0
CAG A:GTQ370 4.8 25.5 1.0
CZ A:ARG83 4.8 30.9 1.0
CD2 A:LEU176 5.0 21.1 1.0

Reference:

M.Ferraroni, I.Matera, S.Burger, S.Reichert, L.Steimer, A.Scozzafava, A.Stolz, F.Briganti. The Salicylate 1,2-Dioxygenase As A Model For A Conventional Gentisate 1,2-Dioxygenase: Crystal Structures of the G106A Mutant and Its Adducts with Gentisate and Salicylate. Febs J. V. 280 1643 2013.
ISSN: ISSN 1742-4658
PubMed: 23384287
DOI: 10.1111/FEBS.12173
Page generated: Tue Aug 5 05:00:54 2025

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