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

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

All present enzymatic activity of Crystal Structure of Salicylate 1,2-Dioxygenase G106A Mutant From Pseudoaminobacter Salicylatoxidans in Complex with Salicylate:
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 Salicylate, PDB code: 3nvc 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 / 2.45
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.273, 86.977, 167.626, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 27.2

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 Salicylate (pdb code 3nvc). 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 Salicylate, PDB code: 3nvc:

Iron binding site 1 out of 1 in 3nvc

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


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

b:49.9
occ:1.00
 C1' A:SAL370 2.0 61.8 1.0
O2' A:SAL370 2.1 57.2 1.0
NE2 A:HIS119 2.1 55.8 1.0
NE2 A:HIS160 2.2 41.9 1.0
O1' A:SAL370 2.2 58.6 1.0
NE2 A:HIS121 2.3 43.7 1.0
CD2 A:HIS119 2.9 53.3 1.0
CE1 A:HIS160 3.0 38.6 1.0
C1 A:SAL370 3.0 64.2 1.0
CD2 A:HIS121 3.1 45.2 1.0
CE1 A:HIS119 3.2 52.1 1.0
C6 A:SAL370 3.3 66.1 1.0
CE1 A:HIS121 3.3 41.5 1.0
CD2 A:HIS160 3.4 42.4 1.0
CG A:HIS119 4.1 52.0 1.0
ND1 A:HIS160 4.2 38.0 1.0
ND1 A:HIS119 4.2 51.0 1.0
CG A:HIS121 4.3 44.8 1.0
ND1 A:HIS121 4.4 45.3 1.0
C2 A:SAL370 4.4 67.5 1.0
CG A:HIS160 4.4 41.5 1.0
O A:HOH415 4.7 36.6 1.0
C5 A:SAL370 4.7 68.6 1.0
O2 A:SAL370 4.7 70.9 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: Sun Aug 4 16:43:25 2024

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