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Iron in PDB 2buv: Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate

Enzymatic activity of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate

All present enzymatic activity of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate:
1.13.11.3;

Protein crystallography data

The structure of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate, PDB code: 2buv 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 (%) 17.4 / 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 R457S in Complex with Protocatechuate (pdb code 2buv). 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 R457S in Complex with Protocatechuate, PDB code: 2buv:

Iron binding site 1 out of 1 in 2buv

Go back to Iron Binding Sites List in 2buv
Iron binding site 1 out of 1 in the Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate


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 R457S in Complex with Protocatechuate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1541

b:20.4
occ:1.00
 OH B:TYR408 1.8 18.4 1.0
O4 B:DHB1542 2.0 23.8 1.0
O3 B:DHB1542 2.0 22.8 1.0
NE2 B:HIS462 2.1 15.7 1.0
NE2 B:HIS460 2.1 15.0 1.0
C4 B:DHB1542 2.7 24.5 1.0
C3 B:DHB1542 2.8 23.7 1.0
CZ B:TYR408 3.0 18.9 1.0
CE1 B:HIS460 3.0 15.2 1.0
CE1 B:HIS462 3.1 19.1 1.0
CD2 B:HIS462 3.1 17.6 1.0
CD2 B:HIS460 3.3 14.7 1.0
CE2 B:TYR408 3.7 19.9 1.0
CE1 B:TYR408 4.0 19.5 1.0
C5 B:DHB1542 4.1 23.7 1.0
C2 B:DHB1542 4.1 22.7 1.0
O B:HOH2095 4.1 16.1 1.0
ND1 B:HIS460 4.2 16.6 1.0
ND1 B:HIS462 4.2 15.9 1.0
O B:HOH2140 4.2 28.6 1.0
CG B:HIS462 4.3 16.7 1.0
O A:HOH2008 4.3 21.9 1.0
CG B:HIS460 4.3 14.8 1.0
O B:HOH2008 4.8 24.6 1.0
CD2 B:TYR447 4.8 21.8 1.0
OE1 B:GLN477 4.8 25.8 1.0
CD2 B:TYR408 5.0 18.8 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: Sat Aug 3 19:50:40 2024

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