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Iron in PDB 1dlq: Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury

Enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury

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

Protein crystallography data

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury, PDB code: 1dlq 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 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.700, 87.600, 84.000, 90.00, 96.50, 90.00
R / Rfree (%) 18.8 / 22.4

Other elements in 1dlq:

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury also contains other interesting chemical elements:

Mercury (Hg) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury (pdb code 1dlq). 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 Inhibited By Bound Mercury, PDB code: 1dlq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dlq

Go back to Iron Binding Sites List in 1dlq
Iron binding site 1 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


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 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:18.8
occ:1.00
OH A:TYR164 1.9 20.2 1.0
NE2 A:HIS226 2.0 16.8 1.0
OH A:TYR200 2.2 28.6 1.0
O A:HOH501 2.3 17.2 1.0
NE2 A:HIS224 2.3 15.6 1.0
CZ A:TYR164 3.0 20.0 1.0
CE1 A:HIS226 3.0 16.5 1.0
CD2 A:HIS226 3.1 15.7 1.0
CE1 A:HIS224 3.2 14.5 1.0
CZ A:TYR200 3.3 28.2 1.0
CD2 A:HIS224 3.3 14.9 1.0
NH1 A:ARG221 3.6 22.5 1.0
CE2 A:TYR200 3.7 27.7 1.0
CE1 A:TYR164 3.8 19.8 1.0
CE2 A:TYR164 3.8 19.1 1.0
ND1 A:HIS226 4.1 15.6 1.0
CG A:HIS226 4.2 16.2 1.0
O A:HOH502 4.2 7.4 1.0
O A:HOH545 4.3 12.2 1.0
ND1 A:HIS224 4.3 14.7 1.0
CG A:HIS224 4.4 14.6 1.0
CE1 A:TYR200 4.6 27.3 1.0
CZ A:ARG221 4.6 21.6 1.0
CD1 A:LEU109 4.7 16.3 1.0

Iron binding site 2 out of 2 in 1dlq

Go back to Iron Binding Sites List in 1dlq
Iron binding site 2 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


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 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe400

b:19.7
occ:1.00
OH B:TYR164 1.9 15.6 1.0
NE2 B:HIS226 2.1 11.6 1.0
NE2 B:HIS224 2.2 15.3 1.0
OH B:TYR200 2.2 28.7 1.0
O B:HOH503 2.6 20.0 1.0
CZ B:TYR164 3.0 16.6 1.0
CE1 B:HIS224 3.0 14.7 1.0
CD2 B:HIS226 3.0 11.0 1.0
CE1 B:HIS226 3.1 10.9 1.0
CD2 B:HIS224 3.2 14.3 1.0
CZ B:TYR200 3.3 28.5 1.0
NH1 B:ARG221 3.4 24.3 1.0
CE2 B:TYR200 3.7 28.3 1.0
CE1 B:TYR164 3.8 16.1 1.0
CE2 B:TYR164 3.8 16.9 1.0
ND1 B:HIS226 4.2 11.1 1.0
O B:HOH532 4.2 8.7 1.0
ND1 B:HIS224 4.2 14.6 1.0
CG B:HIS226 4.2 11.4 1.0
O B:HOH504 4.2 18.4 1.0
CG B:HIS224 4.3 14.3 1.0
CZ B:ARG221 4.5 23.9 1.0
CE1 B:TYR200 4.5 28.0 1.0

Reference:

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
Page generated: Sun Dec 13 14:10:37 2020

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