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Iron in PDB 2buy: Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol

Enzymatic activity of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol

All present enzymatic activity of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol:
1.13.11.3;

Protein crystallography data

The structure of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol, PDB code: 2buy 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 (%) 17.5 / 20.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol (pdb code 2buy). 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 Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol, PDB code: 2buy:

Iron binding site 1 out of 1 in 2buy

Go back to Iron Binding Sites List in 2buy
Iron binding site 1 out of 1 in the Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H 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 Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with Catechol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1541

b:27.0
occ:1.00
OH B:TYR408 1.9 25.8 1.0
O4 B:CAQ1542 2.0 48.2 1.0
O3 B:CAQ1542 2.0 48.1 1.0
NE2 B:HIS462 2.2 18.4 1.0
NE2 B:HIS460 2.2 16.3 1.0
C4 B:CAQ1542 2.7 48.5 1.0
C3 B:CAQ1542 2.8 46.8 1.0
CE1 B:HIS462 3.0 19.1 1.0
CZ B:TYR408 3.1 26.5 1.0
CE1 B:HIS460 3.1 14.7 1.0
CD2 B:HIS460 3.2 15.5 1.0
CD2 B:HIS462 3.3 19.5 1.0
O B:HOH2145 3.3 31.8 1.0
CE2 B:TYR408 3.8 26.9 1.0
CE1 B:TYR408 4.0 26.5 1.0
C5 B:CAQ1542 4.1 48.5 1.0
C2 B:CAQ1542 4.1 47.0 1.0
O A:HOH2012 4.2 21.8 1.0
ND1 B:HIS462 4.2 18.7 1.0
NH1 B:ARG457 4.2 19.5 1.0
O B:HOH2101 4.2 18.3 1.0
ND1 B:HIS460 4.3 17.0 1.0
CG B:HIS460 4.4 15.0 1.0
CG B:HIS462 4.4 18.4 1.0
NE2 B:GLN477 4.8 16.9 1.0

Reference:

M.W.Vetting, M.W.Vetting, M.P.Valley, D.A.D'argenio, L.N.Ornston, J.D.Lipscomb, D.H.Ohlendorf. N/A N/A.
Page generated: Sat Aug 3 19:51:25 2024

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