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Iron in PDB 4fag: Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate

Enzymatic activity of Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate

All present enzymatic activity of Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate:
1.13.11.4;

Protein crystallography data

The structure of Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate, PDB code: 4fag 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) 38.90 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 75.351, 87.908, 167.078, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 26.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate (pdb code 4fag). 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 the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate, PDB code: 4fag:

Iron binding site 1 out of 1 in 4fag

Go back to Iron Binding Sites List in 4fag
Iron binding site 1 out of 1 in the Crystal Structure of the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant 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 the Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans W104Y Mutant in Complex with Gentisate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:51.2
occ:1.00
 OAD A:GTQ402 1.6 74.5 1.0
NE2 A:HIS119 2.0 57.1 1.0
NE2 A:HIS160 2.3 44.7 1.0
OAB A:GTQ402 2.3 69.6 1.0
NE2 A:HIS121 2.4 36.2 1.0
CAJ A:GTQ402 2.9 75.8 1.0
CE1 A:HIS119 2.9 56.5 1.0
CE1 A:HIS160 3.1 46.0 1.0
CD2 A:HIS119 3.1 54.6 1.0
CAH A:GTQ402 3.2 72.5 1.0
CD2 A:HIS121 3.3 38.6 1.0
CD2 A:HIS160 3.4 47.7 1.0
CE1 A:HIS121 3.4 37.6 1.0
CAK A:GTQ402 3.5 74.7 1.0
CAF A:GTQ402 4.0 77.5 1.0
ND1 A:HIS119 4.0 55.6 1.0
CG A:HIS119 4.2 54.6 1.0
ND1 A:HIS160 4.3 46.7 1.0
NH2 A:ARG83 4.3 60.0 1.0
OAA A:GTQ402 4.4 71.0 1.0
CG A:HIS160 4.4 48.4 1.0
CG A:HIS121 4.5 40.6 1.0
ND1 A:HIS121 4.5 39.9 1.0
NH1 A:ARG127 4.6 56.4 1.0
NE A:ARG83 4.8 63.2 1.0
NH2 A:ARG127 4.8 58.8 1.0
CAG A:GTQ402 4.9 75.7 1.0
CZ A:ARG83 4.9 62.4 1.0

Reference:

M.Ferraroni, L.Steimer, I.Matera, S.Burger, A.Scozzafava, A.Stolz, F.Briganti. The Generation of A 1-Hydroxy-2-Naphthoate 1,2-Dioxygenase By Single Point Mutations of Salicylate 1,2-Dioxygenase - Rational Design of Mutants and the Crystal Structures of the A85H and W104Y Variants. J.Struct.Biol. V. 180 563 2012.
ISSN: ISSN 1047-8477
PubMed: 22960182
DOI: 10.1016/J.JSB.2012.08.007
Page generated: Mon Aug 5 02:07:57 2024

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