Atomistry » Iron » PDB 1dj7-1dry » 1dlm
Atomistry »
  Iron »
    PDB 1dj7-1dry »
      1dlm »

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: Sat Aug 3 03:48:37 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy