Iron in PDB 1knd: Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition

All present enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition:
1.13.11.39;

The structure of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition, PDB code: 1knd was solved by S.Han, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	122.800, 122.800, 110.600, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.3

The binding sites of Iron atom in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition (pdb code 1knd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition, PDB code: 1knd:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition


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-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:20.1 occ:1.00 OE2 A:GLU260 2.0 14.7 1.0 NE2 A:HIS146 2.1 14.6 1.0 O A:HOH3012 2.1 16.2 0.5 NE2 A:HIS210 2.3 17.1 1.0 O A:HOH9001 2.3 29.3 0.5 O3 A:CAQ301 2.3 24.0 0.5 O4 A:CAQ301 2.4 20.6 0.5 O A:HOH3001 2.5 9.2 0.5 CE1 A:HIS146 2.9 11.9 1.0 CD A:GLU260 3.1 12.4 1.0 CE1 A:HIS210 3.1 17.2 1.0 C3 A:CAQ301 3.1 23.1 0.5 C4 A:CAQ301 3.2 22.2 0.5 CD2 A:HIS146 3.3 15.9 1.0 CD2 A:HIS210 3.4 15.3 1.0 O A:HOH9002 3.4 20.7 0.5 OE1 A:GLU260 3.6 15.4 1.0 OH A:TYR250 3.9 17.4 1.0 NE2 A:HIS195 4.0 15.9 1.0 ND1 A:HIS146 4.1 14.0 1.0 CB A:MET212 4.3 11.1 1.0 CG A:HIS146 4.3 13.9 1.0 CG A:GLU260 4.3 10.1 1.0 ND1 A:HIS210 4.3 19.0 1.0 CB A:GLU260 4.5 11.0 1.0 C2 A:CAQ301 4.5 23.0 0.5 CG A:MET212 4.5 13.0 1.0 CG A:HIS210 4.5 16.3 1.0 C5 A:CAQ301 4.5 22.1 0.5 O A:HOH4014 4.5 15.6 0.5 CE1 A:HIS195 4.5 14.8 1.0 NE2 A:HIS241 4.7 18.9 1.0 CZ A:TYR250 4.7 15.4 1.0 CE2 A:TYR250 4.9 16.0 1.0 CG2 A:VAL148 4.9 18.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with Catechol Under Anaerobic Condition within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:60.5 occ:0.50 NE2 A:HIS189 2.5 20.3 1.0 CE1 A:HIS189 3.4 19.8 1.0 CD2 A:HIS189 3.5 18.7 1.0 CG A:GLN168 4.0 29.1 1.0 CB A:GLN168 4.0 21.7 1.0 ND1 A:HIS189 4.6 18.8 1.0 CG A:HIS189 4.7 18.8 1.0 CG1 A:VAL268 4.8 27.6 1.0

F.H.Vaillancourt, S.Han, P.D.Fortin, J.T.Bolin, L.D.Eltis. Molecular Basis For the Stabilization and Inhibition of 2, 3-Dihydroxybiphenyl 1,2-Dioxygenase By T-Butanol. J.Biol.Chem. V. 273 34887 1998.
ISSN: ISSN 0021-9258
PubMed: 9857017
DOI: 10.1074/JBC.273.52.34887