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

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

All present enzymatic activity of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R133H in Complex with 4-Nitrocatechol:
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 4-Nitrocatechol, PDB code: 2buz 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 (°) 145.090, 145.090, 145.090, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.2

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 4-Nitrocatechol (pdb code 2buz). 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 4-Nitrocatechol, PDB code: 2buz:

Iron binding site 1 out of 1 in 2buz

Go back to Iron Binding Sites List in 2buz
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 4-Nitrocatechol


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 4-Nitrocatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1541

b:30.2
occ:1.00
 O8 B:4NC1542 2.0 34.7 1.0
OH B:TYR408 2.0 21.9 1.0
OH B:TYR447 2.1 25.9 1.0
NE2 B:HIS462 2.2 21.6 1.0
NE2 B:HIS460 2.2 19.5 1.0
O7 B:4NC1542 2.3 29.9 1.0
C2 B:4NC1542 2.8 36.0 1.0
C1 B:4NC1542 2.9 35.2 1.0
CE1 B:HIS460 3.0 19.2 1.0
CZ B:TYR408 3.1 22.9 1.0
CE1 B:HIS462 3.1 20.9 1.0
CD2 B:HIS462 3.3 21.0 1.0
CZ B:TYR447 3.3 25.4 1.0
CD2 B:HIS460 3.3 19.7 1.0
CE2 B:TYR408 3.6 23.1 1.0
CE2 B:TYR447 3.8 25.8 1.0
C3 B:4NC1542 4.0 37.2 1.0
CE1 B:TYR408 4.1 22.9 1.0
O B:HOH2069 4.1 20.6 1.0
C6 B:4NC1542 4.2 35.8 1.0
NH1 B:ARG457 4.2 22.8 1.0
ND1 B:HIS460 4.2 19.7 1.0
O A:HOH2009 4.2 24.5 1.0
ND1 B:HIS462 4.2 20.8 1.0
CG B:HIS462 4.4 19.6 1.0
CE1 B:TYR447 4.4 24.6 1.0
CG B:HIS460 4.4 17.9 1.0
CD2 B:TYR408 4.9 25.3 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 19:51:44 2024

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