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Iron in PDB 1dlm: Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data

Enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data

All present enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data:
1.13.11.1;

Protein crystallography data

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data, PDB code: 1dlm 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 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.600, 87.600, 84.200, 90.00, 96.30, 90.00
R / Rfree (%) 19.6 / 24.3

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data (pdb code 1dlm). 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 Calcoaceticus Native Data, PDB code: 1dlm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dlm

Go back to Iron Binding Sites List in 1dlm
Iron binding site 1 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data


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 Calcoaceticus Native Data within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:21.7
occ:1.00
OH A:TYR164 1.8 19.3 1.0
NE2 A:HIS226 2.0 13.5 1.0
NE2 A:HIS224 2.2 14.1 1.0
OH A:TYR200 2.3 33.7 1.0
O A:HOH501 2.4 15.9 1.0
CE1 A:HIS226 2.9 13.0 1.0
CZ A:TYR164 2.9 17.9 1.0
CD2 A:HIS226 3.0 14.7 1.0
CE1 A:HIS224 3.1 11.0 1.0
CD2 A:HIS224 3.2 12.4 1.0
CZ A:TYR200 3.3 35.4 1.0
CE2 A:TYR200 3.5 34.8 1.0
CE1 A:TYR164 3.7 17.7 1.0
CE2 A:TYR164 3.8 17.1 1.0
NH1 A:ARG221 3.9 25.8 1.0
ND1 A:HIS226 4.0 14.4 1.0
CG A:HIS226 4.1 16.6 1.0
O A:HOH523 4.2 15.4 1.0
ND1 A:HIS224 4.2 11.6 1.0
O A:HOH502 4.3 13.0 1.0
CG A:HIS224 4.3 12.4 1.0
CE1 A:TYR200 4.6 33.3 1.0
CD1 A:LEU109 4.8 17.9 1.0
CD2 A:TYR200 4.8 32.4 1.0
O A:HOH572 4.9 23.6 1.0
CZ A:ARG221 4.9 23.9 1.0
CD1 A:TYR164 5.0 19.8 1.0

Iron binding site 2 out of 2 in 1dlm

Go back to Iron Binding Sites List in 1dlm
Iron binding site 2 out of 2 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Calcoaceticus Native Data


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 Calcoaceticus Native Data within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe400

b:17.9
occ:1.00
OH B:TYR164 1.8 15.1 1.0
NE2 B:HIS226 2.0 10.4 1.0
NE2 B:HIS224 2.1 14.5 1.0
OH B:TYR200 2.2 31.0 1.0
O B:HOH503 2.4 32.3 1.0
CZ B:TYR164 3.0 15.6 1.0
CE1 B:HIS226 3.0 11.6 1.0
CE1 B:HIS224 3.0 16.3 1.0
CD2 B:HIS226 3.0 11.6 1.0
CD2 B:HIS224 3.2 14.6 1.0
CZ B:TYR200 3.3 30.0 1.0
NH1 B:ARG221 3.6 22.6 1.0
CE2 B:TYR200 3.7 31.7 1.0
CE1 B:TYR164 3.7 16.3 1.0
CE2 B:TYR164 3.9 16.9 1.0
ND1 B:HIS226 4.1 11.2 1.0
O B:HOH530 4.1 17.9 1.0
CG B:HIS226 4.1 12.0 1.0
ND1 B:HIS224 4.2 14.8 1.0
CG B:HIS224 4.3 15.4 1.0
O B:HOH504 4.3 14.1 1.0
CE1 B:TYR200 4.6 30.4 1.0
CZ B:ARG221 4.7 22.3 1.0
O B:HOH542 4.9 18.6 1.0
CD B:ARG221 5.0 16.2 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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