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Iron in PDB 2buq: Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol

Enzymatic activity of Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol

All present enzymatic activity of Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol:
1.13.11.3;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol, PDB code: 2buq was solved by M.W.Vetting, M.P.Valley, D.A.D'argenio, L.N.Ornston, J.D.Lipscomb, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.80
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 144.700, 144.700, 144.700, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 19.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol (pdb code 2buq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol, PDB code: 2buq:

Iron binding site 1 out of 1 in 2buq

Go back to Iron Binding Sites List in 2buq
Iron binding site 1 out of 1 in the Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Wild-Type Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 in Complex with Catechol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1541

b:24.8
occ:1.00
 OH B:TYR408 1.9 28.6 1.0
O4 B:CAQ1542 2.0 38.6 1.0
O3 B:CAQ1542 2.1 40.1 1.0
NE2 B:HIS462 2.1 18.8 1.0
NE2 B:HIS460 2.1 17.3 1.0
C4 B:CAQ1542 2.7 39.6 1.0
C3 B:CAQ1542 2.8 37.8 1.0
CE1 B:HIS460 3.0 16.5 1.0
CE1 B:HIS462 3.0 20.2 1.0
CZ B:TYR408 3.1 28.8 1.0
CD2 B:HIS462 3.2 19.8 1.0
CD2 B:HIS460 3.2 18.1 1.0
CE2 B:TYR408 3.8 28.8 1.0
O B:HOH2155 3.9 31.2 1.0
CE1 B:TYR408 4.0 27.9 1.0
C5 B:CAQ1542 4.1 39.7 1.0
C2 B:CAQ1542 4.1 38.7 1.0
ND1 B:HIS460 4.2 18.1 1.0
O B:HOH2102 4.2 21.9 1.0
ND1 B:HIS462 4.2 18.3 1.0
NH1 B:ARG457 4.2 20.4 1.0
CG B:HIS462 4.3 18.8 1.0
CG B:HIS460 4.3 16.2 1.0
O A:HOH2010 4.3 23.2 1.0
OE1 B:GLN477 4.8 21.5 1.0

Reference:

C.K.Brown, M.W.Vetting, C.A.Earhart, D.H.Ohlendorf. Biophysical Analyses of Designed and Selected Mutants of Protocatechuate 3,4-Dioxygenase Annu.Rev.Microbiol. V. 58 555 2004.
ISSN: ISSN 0066-4227
PubMed: 15487948
DOI: 10.1146/ANNUREV.MICRO.57.030502.090927
Page generated: Thu Jul 17 00:02:14 2025

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