Iron in PDB 1dlt: Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol

All present enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol:
1.13.11.1;

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol, PDB code: 1dlt was solved by M.W.Vetting, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.800, 87.500, 84.400, 90.00, 96.30, 90.00
R / Rfree (%)	18.9 / 22.8

The binding sites of Iron atom in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol (pdb code 1dlt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol, PDB code: 1dlt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:18.7 occ:1.00 O4 A:CAQ401 1.7 19.9 0.7 OH A:TYR164 2.0 17.7 1.0 NE2 A:HIS226 2.0 13.2 1.0 NE2 A:HIS224 2.1 16.9 1.0 O3 A:CAQ401 2.4 17.6 0.7 O A:HOH501 2.4 5.5 0.3 C4 A:CAQ401 2.7 16.8 0.7 C3 A:CAQ401 2.9 17.2 0.7 CD2 A:HIS226 2.9 11.7 1.0 CE1 A:HIS226 3.0 12.2 1.0 CZ A:TYR164 3.0 16.8 1.0 CD2 A:HIS224 3.1 12.0 1.0 CE1 A:HIS224 3.2 12.5 1.0 CE1 A:TYR164 3.8 17.2 1.0 CE2 A:TYR164 3.9 16.1 1.0 C5 A:CAQ401 3.9 18.0 0.7 NH1 A:ARG221 4.0 24.2 1.0 O A:HOH528 4.1 12.9 1.0 ND1 A:HIS226 4.1 13.0 1.0 CG A:HIS226 4.1 14.2 1.0 CG A:HIS224 4.2 11.3 1.0 ND1 A:HIS224 4.2 12.1 1.0 C2 A:CAQ401 4.3 16.8 0.7 O A:HOH502 4.4 13.2 1.0

Iron binding site 2 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound Catechol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe400 b:16.2 occ:1.00 OH B:TYR164 1.9 15.0 1.0 O4 B:CAQ401 1.9 15.0 0.7 NE2 B:HIS224 2.1 11.2 1.0 NE2 B:HIS226 2.1 9.0 1.0 O3 B:CAQ401 2.2 20.0 0.7 O B:HOH503 2.5 13.2 0.3 C4 B:CAQ401 2.8 16.9 0.7 C3 B:CAQ401 2.9 18.1 0.7 CZ B:TYR164 3.0 15.1 1.0 CE1 B:HIS224 3.0 11.7 1.0 CD2 B:HIS226 3.0 10.4 1.0 CD2 B:HIS224 3.1 11.4 1.0 CE1 B:HIS226 3.2 10.6 1.0 CE1 B:TYR164 3.7 14.6 1.0 CE2 B:TYR164 3.9 16.3 1.0 O B:HOH515 4.0 10.6 1.0 NH1 B:ARG221 4.1 28.3 1.0 C5 B:CAQ401 4.1 17.2 0.7 ND1 B:HIS224 4.1 11.0 1.0 CG B:HIS226 4.2 10.2 1.0 ND1 B:HIS226 4.2 11.7 1.0 CG B:HIS224 4.2 12.1 1.0 C2 B:CAQ401 4.3 19.8 0.7 O B:HOH504 4.4 13.0 1.0 CD1 B:TYR164 5.0 14.5 1.0

M.W.Vetting, D.H.Ohlendorf. The 1.8 A Crystal Structure of Catechol 1,2-Dioxygenase Reveals A Novel Hydrophobic Helical Zipper As A Subunit Linker. Structure Fold.Des. V. 8 429 2000.
ISSN: ISSN 0969-2126
PubMed: 10801478
DOI: 10.1016/S0969-2126(00)00122-2