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Iron in PDB 3nkt: Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate

Enzymatic activity of Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate

All present enzymatic activity of Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate:
1.13.11.4;

Protein crystallography data

The structure of Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate, PDB code: 3nkt 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 / 2.35
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.149, 86.131, 166.943, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate (pdb code 3nkt). 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 From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate, PDB code: 3nkt:

Iron binding site 1 out of 1 in 3nkt

Go back to Iron Binding Sites List in 3nkt
Iron binding site 1 out of 1 in the Crystal Structure of Salicylate 1,2-Dioxygenase From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate


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 From Pseudoaminobacter Salicylatoxidans Adducts with Naphthoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe369

b:33.5
occ:1.00
 O1 A:1HN370 1.6 40.7 1.0
NE2 A:HIS119 2.0 41.8 1.0
NE2 A:HIS160 2.2 35.8 1.0
NE2 A:HIS121 2.2 33.7 1.0
O3 A:1HN370 2.3 37.8 1.0
C1 A:1HN370 2.9 41.9 1.0
CD2 A:HIS119 2.9 40.1 1.0
CE1 A:HIS119 3.0 42.1 1.0
CE1 A:HIS160 3.0 33.8 1.0
CD2 A:HIS121 3.1 33.9 1.0
CE1 A:HIS121 3.2 32.1 1.0
CD2 A:HIS160 3.3 35.3 1.0
C9 A:1HN370 3.3 40.2 1.0
C2 A:1HN370 3.6 41.3 1.0
ND1 A:HIS119 4.1 41.2 1.0
CG A:HIS119 4.1 41.0 1.0
C8A A:1HN370 4.1 43.4 1.0
ND1 A:HIS160 4.1 35.3 1.0
ND1 A:HIS121 4.3 34.0 1.0
NH2 A:ARG127 4.3 36.7 1.0
CG A:HIS121 4.3 34.3 1.0
CG A:HIS160 4.3 34.2 1.0
NH2 A:ARG83 4.4 44.7 1.0
C8 A:1HN370 4.4 43.9 1.0
O2 A:1HN370 4.5 39.4 1.0
NE A:ARG83 4.6 44.0 1.0
CZ A:ARG83 4.8 44.7 1.0
C3 A:1HN370 4.9 42.8 1.0

Reference:

M.Ferraroni, I.Matera, L.Steimer, S.Burger, A.Scozzafava, A.Stolz, F.Briganti. Crystal Structures of Salicylate 1,2-Dioxygenase-Substrates Adducts: A Step Towards the Comprehension of the Structural Basis For Substrate Selection in Class III Ring Cleaving Dioxygenases. J.Struct.Biol. V. 177 431 2012.
ISSN: ISSN 1047-8477
PubMed: 22155290
DOI: 10.1016/J.JSB.2011.11.026
Page generated: Sun Aug 4 16:27:54 2024

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