Iron in PDB 1eiq: 2,3-Dihydroxybiphenyl-1,2-Dioxygenase

All present enzymatic activity of 2,3-Dihydroxybiphenyl-1,2-Dioxygenase:
1.13.11.39;

The structure of 2,3-Dihydroxybiphenyl-1,2-Dioxygenase, PDB code: 1eiq was solved by T.Senda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.00 / 2.00
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.890, 121.890, 108.800, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22.8

The binding sites of Iron atom in the 2,3-Dihydroxybiphenyl-1,2-Dioxygenase (pdb code 1eiq). 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 2,3-Dihydroxybiphenyl-1,2-Dioxygenase, PDB code: 1eiq:

Iron binding site 1 out of 1 in the 2,3-Dihydroxybiphenyl-1,2-Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2,3-Dihydroxybiphenyl-1,2-Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:31.4 occ:1.00 OE1 A:GLU260 2.1 21.7 1.0 O A:HOH455 2.2 24.3 1.0 NE2 A:HIS145 2.3 21.1 1.0 NE2 A:HIS209 2.5 23.7 1.0 O A:HOH430 2.7 39.0 1.0 CE1 A:HIS145 3.1 15.9 1.0 CE1 A:HIS209 3.1 19.3 1.0 CD A:GLU260 3.2 16.1 1.0 CD2 A:HIS145 3.5 23.8 1.0 CD2 A:HIS209 3.7 22.9 1.0 OH A:TYR249 3.7 21.4 1.0 OE2 A:GLU260 3.7 17.5 1.0 NE2 A:HIS194 4.2 20.6 1.0 CB A:MET211 4.3 16.9 1.0 ND1 A:HIS145 4.3 22.0 1.0 ND1 A:HIS209 4.4 23.4 1.0 CG A:GLU260 4.5 16.2 1.0 CG A:HIS145 4.5 21.4 1.0 CB A:GLU260 4.6 12.3 1.0 CZ A:TYR249 4.6 18.6 1.0 CG A:MET211 4.6 17.0 1.0 CE1 A:HIS194 4.6 15.4 1.0 NE2 A:HIS240 4.6 19.9 1.0 CE1 A:TYR249 4.7 12.6 1.0 CG A:HIS209 4.7 24.7 1.0 CG2 A:VAL147 4.7 14.0 1.0 O A:HOH327 4.8 35.4 1.0

Y.Uragami, T.Senda, K.Sugimoto, N.Sato, V.Nagarajan, E.Masai, M.Fukuda, Y.Mitsu. Crystal Structures of Substrate Free and Complex Forms of Reactivated Bphc, An Extradiol Type Ring-Cleavage Dioxygenase. J.Inorg.Biochem. V. 83 269 2001.
ISSN: ISSN 0162-0134
PubMed: 11293547
DOI: 10.1016/S0162-0134(00)00172-0