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Iron in PDB 1kw3: Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution

Enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution

All present enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution:
1.13.11.39;

Protein crystallography data

The structure of Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution, PDB code: 1kw3 was solved by N.Sato, Y.Uragami, T.Nishizaki, Y.Takahashi, G.Sazaki, K.Sugimoto, T.Nonaka, E.Masai, M.Fukuda, T.Senda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.71 / 1.45
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 121.760, 121.760, 108.910, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 17.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution (pdb code 1kw3). 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 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution, PDB code: 1kw3:

Iron binding site 1 out of 1 in 1kw3

Go back to Iron Binding Sites List in 1kw3
Iron binding site 1 out of 1 in the Crystal Structure of 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution


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 2,3-Dihydroxybiphenyal Dioxygenase (Bphc) at 1.45 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:7.3
occ:1.00
OE1 B:GLU260 2.0 9.9 1.0
NE2 B:HIS145 2.1 7.9 1.0
NE2 B:HIS209 2.1 8.6 1.0
O B:HOH800 2.2 12.5 1.0
O B:HOH564 2.3 15.0 1.0
CE1 B:HIS145 3.0 10.2 1.0
CE1 B:HIS209 3.0 7.7 1.0
CD B:GLU260 3.1 8.7 1.0
CD2 B:HIS145 3.2 8.1 1.0
CD2 B:HIS209 3.2 6.8 1.0
OH B:TYR249 3.5 12.4 1.0
OE2 B:GLU260 3.6 9.2 1.0
NE2 B:HIS194 4.1 9.7 1.0
O B:HOH801 4.1 21.6 1.0
ND1 B:HIS145 4.1 11.4 1.0
CB B:MET211 4.2 8.0 1.0
ND1 B:HIS209 4.2 8.1 1.0
CG B:HIS145 4.3 8.6 1.0
CG B:HIS209 4.3 8.0 1.0
CG B:GLU260 4.4 7.6 1.0
CZ B:TYR249 4.5 10.8 1.0
CG B:MET211 4.5 8.2 1.0
CB B:GLU260 4.5 7.5 1.0
CE1 B:TYR249 4.7 9.5 1.0
NE2 B:HIS240 4.7 11.3 1.0
CG2 B:VAL147 4.7 11.4 1.0
CE1 B:HIS194 4.7 9.9 1.0
O B:HOH676 4.7 21.7 1.0

Reference:

N.Sato, Y.Uragami, T.Nishizaki, Y.Takahashi, G.Sazaki, K.Sugimoto, T.Nonaka, E.Masai, M.Fukuda, T.Senda. Crystal Structures of the Reaction Intermediate and Its Homologue of An Extradiol-Cleaving Catecholic Dioxygenase J.Mol.Biol. V. 321 621 2002.
ISSN: ISSN 0022-2836
PubMed: 12206778
DOI: 10.1016/S0022-2836(02)00673-3
Page generated: Sun Dec 13 14:21:23 2020

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