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Iron in PDB 3nst: Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans

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

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

Protein crystallography data

The structure of Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans, PDB code: 3nst 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) 83.92 / 2.40
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.715, 87.046, 167.920, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 21.9

Iron Binding Sites:

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

Iron binding site 1 out of 1 in 3nst

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


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe369

b:35.1
occ:1.00
 NE2 A:HIS119 2.1 37.6 1.0
NE2 A:HIS160 2.1 33.5 1.0
O1 A:GOL375 2.2 41.8 1.0
NE2 A:HIS121 2.3 32.4 1.0
C3 A:GOL375 2.3 35.6 0.5
O3 A:GOL375 2.5 24.3 0.5
O3 A:GOL375 2.5 27.7 0.5
C3 A:GOL375 2.7 32.5 0.5
CE1 A:HIS119 2.9 37.0 1.0
CE1 A:HIS160 3.0 31.9 1.0
CD2 A:HIS160 3.2 35.8 1.0
CD2 A:HIS121 3.2 30.8 1.0
C1 A:GOL375 3.2 37.9 1.0
CE1 A:HIS121 3.3 27.1 1.0
CD2 A:HIS119 3.3 38.6 1.0
C2 A:GOL375 3.3 37.8 1.0
ND1 A:HIS119 4.1 39.4 1.0
ND1 A:HIS160 4.2 30.9 1.0
CG A:HIS160 4.3 33.4 1.0
CG A:HIS119 4.3 39.3 1.0
O A:HOH437 4.4 28.5 1.0
ND1 A:HIS121 4.4 30.1 1.0
CG A:HIS121 4.4 31.1 1.0
O2 A:GOL375 4.5 40.5 1.0
O A:HOH464 4.6 55.5 1.0
O A:HOH701 4.9 50.9 1.0
NH2 A:ARG127 5.0 35.7 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 04:54:47 2025

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