Atomistry » Iron » PDB 2bmo-2c1v » 2but
Atomistry »
  Iron »
    PDB 2bmo-2c1v »
      2but »

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

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

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

Protein crystallography data

The structure of Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S - Apo, PDB code: 2but 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 / 1.85
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 144.870, 144.870, 144.870, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.5

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Protocatechuate 3,4-Dioxygenase From Acinetobacter Sp. ADP1 Mutant R457S - Apo (pdb code 2but). 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 - Apo, PDB code: 2but:

Iron binding site 1 out of 1 in 2but

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


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

b:22.1
occ:1.00
 OH B:TYR408 1.8 19.3 1.0
O B:OH1542 2.0 25.0 1.0
OH B:TYR447 2.0 22.6 1.0
NE2 B:HIS460 2.2 17.9 1.0
NE2 B:HIS462 2.2 17.1 1.0
CZ B:TYR408 3.0 21.1 1.0
CE1 B:HIS460 3.0 18.1 1.0
CE1 B:HIS462 3.0 16.8 1.0
CZ B:TYR447 3.2 21.1 1.0
CD2 B:HIS460 3.3 17.9 1.0
CD2 B:HIS462 3.3 18.5 1.0
CE2 B:TYR408 3.6 21.0 1.0
CE2 B:TYR447 3.6 21.2 1.0
CE1 B:TYR408 4.0 20.7 1.0
O B:HOH2096 4.1 18.2 1.0
ND1 B:HIS460 4.2 18.8 1.0
O B:HOH2094 4.2 33.7 1.0
ND1 B:HIS462 4.2 16.5 1.0
O A:HOH2010 4.3 19.4 1.0
CE1 B:TYR447 4.4 20.6 1.0
CG B:HIS460 4.4 17.6 1.0
CG B:HIS462 4.4 17.0 1.0
OE1 B:GLN477 4.7 33.8 1.0
CD2 B:TYR408 4.9 21.6 1.0
CD2 B:TYR447 5.0 20.4 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 19:50:09 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy