Iron in PDB 1dmh: Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound 4-Methylcatechol

All present enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound 4-Methylcatechol:
1.13.11.1;

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound 4-Methylcatechol, PDB code: 1dmh 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 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.800, 88.000, 84.400, 90.00, 96.30, 90.00
R / Rfree (%)	18.5 / 21.8

The binding sites of Iron atom in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound 4-Methylcatechol (pdb code 1dmh). 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 4-Methylcatechol, PDB code: 1dmh:
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 4-Methylcatechol


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 4-Methylcatechol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:16.0 occ:1.00 O4 A:MCT401 1.8 22.5 0.7 OH A:TYR164 1.9 17.4 1.0 NE2 A:HIS224 2.0 12.7 1.0 O3 A:MCT401 2.1 22.3 0.7 NE2 A:HIS226 2.1 12.1 1.0 O A:HOH501 2.6 3.7 0.3 C4 A:MCT401 2.6 21.2 0.7 C3 A:MCT401 2.7 21.4 0.7 CZ A:TYR164 3.0 16.9 1.0 CE1 A:HIS224 3.0 12.0 1.0 CD2 A:HIS224 3.0 10.7 1.0 CD2 A:HIS226 3.1 11.4 1.0 CE1 A:HIS226 3.1 12.1 1.0 CE1 A:TYR164 3.7 16.8 1.0 C5 A:MCT401 3.9 21.7 0.7 CE2 A:TYR164 3.9 16.5 1.0 NH1 A:ARG221 4.0 24.6 1.0 O A:HOH517 4.1 12.9 1.0 C2 A:MCT401 4.1 22.1 0.7 ND1 A:HIS224 4.1 10.4 1.0 CG A:HIS224 4.2 11.3 1.0 ND1 A:HIS226 4.2 11.8 1.0 CG A:HIS226 4.2 12.8 1.0 O A:HOH502 4.4 12.2 1.0 CD1 A:LEU109 4.7 16.5 1.0

Iron binding site 2 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 with Bound 4-Methylcatechol


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 4-Methylcatechol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe400 b:14.1 occ:1.00 O3 B:MCT401 1.8 21.5 0.7 OH B:TYR164 2.0 12.4 1.0 NE2 B:HIS226 2.0 10.6 1.0 NE2 B:HIS224 2.1 10.6 1.0 O4 B:MCT401 2.1 19.6 0.7 O B:HOH503 2.5 5.8 0.3 C3 B:MCT401 2.6 19.7 0.7 C4 B:MCT401 2.7 19.3 0.7 CD2 B:HIS226 2.9 10.1 1.0 CE1 B:HIS226 3.0 11.0 1.0 CE1 B:HIS224 3.0 12.2 1.0 CZ B:TYR164 3.1 11.8 1.0 CD2 B:HIS224 3.1 11.6 1.0 NH1 B:ARG221 3.8 24.3 1.0 CE1 B:TYR164 3.8 12.8 1.0 CE2 B:TYR164 3.9 13.7 1.0 C2 B:MCT401 3.9 20.5 0.7 ND1 B:HIS226 4.1 10.5 1.0 CG B:HIS226 4.1 10.9 1.0 C5 B:MCT401 4.1 19.8 0.7 O B:HOH512 4.1 11.8 1.0 ND1 B:HIS224 4.2 11.3 1.0 CG B:HIS224 4.2 11.3 1.0 O B:HOH504 4.2 11.8 1.0 CZ B:ARG221 5.0 22.6 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