Atomistry » Iron » PDB 3lhs-3m2i » 3lxv
Atomistry »
  Iron »
    PDB 3lhs-3m2i »
      3lxv »

Iron in PDB 3lxv: Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis

Enzymatic activity of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis

All present enzymatic activity of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis:
1.13.11.3;

Protein crystallography data

The structure of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis, PDB code: 3lxv was solved by V.M.Purpero, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.99 / 1.90
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 128.110, 140.590, 167.960, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 24.6

Other elements in 3lxv:

The structure of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis (pdb code 3lxv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis, PDB code: 3lxv:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 3lxv

Go back to Iron Binding Sites List in 3lxv
Iron binding site 1 out of 3 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Fe600

b:27.2
occ:1.00
OH M:TYR408 1.8 30.0 1.0
O8 M:4NC1 2.1 45.0 1.0
NE2 M:HIS462 2.1 23.7 1.0
NE2 M:HIS460 2.1 26.4 1.0
O M:HOH948 2.4 35.4 1.0
O7 M:4NC1 2.4 44.6 1.0
CZ M:TYR408 2.9 28.9 1.0
CE1 M:HIS462 3.0 23.3 1.0
C2 M:4NC1 3.0 44.3 1.0
CE1 M:HIS460 3.1 25.7 1.0
C1 M:4NC1 3.1 44.0 1.0
CD2 M:HIS460 3.2 24.9 1.0
CD2 M:HIS462 3.3 26.3 1.0
CE2 M:TYR408 3.7 27.4 1.0
CE1 M:TYR408 3.8 27.7 1.0
ND1 M:HIS462 4.1 24.8 1.0
NH1 M:ARG457 4.2 23.3 1.0
O M:HOH218 4.2 26.0 1.0
ND1 M:HIS460 4.2 24.8 1.0
C3 M:4NC1 4.3 45.0 1.0
O A:HOH223 4.3 33.6 1.0
CG M:HIS460 4.3 24.6 1.0
CG M:HIS462 4.3 24.0 1.0
C6 M:4NC1 4.4 43.5 1.0
O M:HOH964 4.4 36.9 0.5
OE1 M:GLN477 4.8 25.3 1.0
CD2 M:TYR408 5.0 27.7 1.0

Iron binding site 2 out of 3 in 3lxv

Go back to Iron Binding Sites List in 3lxv
Iron binding site 2 out of 3 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe600

b:27.4
occ:1.00
OH N:TYR408 1.8 30.9 1.0
NE2 N:HIS462 2.1 26.2 1.0
NE2 N:HIS460 2.2 27.0 1.0
O8 N:4NC2 2.2 43.8 0.9
O7 N:4NC2 2.4 43.2 0.9
O N:HOH949 2.4 35.9 1.0
CZ N:TYR408 2.9 29.3 1.0
C2 N:4NC2 3.0 42.0 0.9
C1 N:4NC2 3.0 41.1 0.9
CE1 N:HIS462 3.0 25.5 1.0
CE1 N:HIS460 3.1 26.2 1.0
CD2 N:HIS460 3.2 25.2 1.0
CD2 N:HIS462 3.2 23.9 1.0
CE2 N:TYR408 3.7 26.4 1.0
CE1 N:TYR408 3.8 29.9 1.0
ND1 N:HIS462 4.2 27.0 1.0
NH2 N:ARG457 4.2 25.5 1.0
ND1 N:HIS460 4.3 25.6 1.0
C3 N:4NC2 4.3 42.0 0.9
O B:HOH206 4.3 32.7 1.0
O N:HOH552 4.3 25.4 1.0
CG N:HIS462 4.3 25.6 1.0
CG N:HIS460 4.3 25.2 1.0
C6 N:4NC2 4.4 43.3 0.9
OE1 N:GLN477 4.9 27.7 1.0
CD2 N:TYR408 5.0 27.8 1.0

Iron binding site 3 out of 3 in 3lxv

Go back to Iron Binding Sites List in 3lxv
Iron binding site 3 out of 3 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Fe600

b:28.5
occ:1.00
OH O:TYR408 2.0 32.7 1.0
NE2 O:HIS462 2.1 27.9 1.0
NE2 O:HIS460 2.1 23.5 1.0
O7 O:4NC3 2.3 41.8 1.0
O8 O:4NC3 2.4 44.2 1.0
O O:HOH952 2.5 43.8 1.0
CE1 O:HIS462 3.0 27.5 1.0
CZ O:TYR408 3.0 32.1 1.0
CE1 O:HIS460 3.1 23.9 1.0
C2 O:4NC3 3.1 42.3 1.0
C1 O:4NC3 3.1 41.4 1.0
CD2 O:HIS462 3.1 23.7 1.0
CD2 O:HIS460 3.2 25.1 1.0
CE2 O:TYR408 3.7 32.9 1.0
CE1 O:TYR408 3.8 32.2 1.0
ND1 O:HIS462 4.1 26.6 1.0
NH1 O:ARG457 4.1 22.6 1.0
ND1 O:HIS460 4.2 27.4 1.0
O O:HOH113 4.2 23.5 1.0
CG O:HIS462 4.2 26.1 1.0
CG O:HIS460 4.3 24.6 1.0
O C:HOH818 4.3 29.5 1.0
O O:HOH955 4.3 34.4 0.5
C3 O:4NC3 4.4 41.0 1.0
C6 O:4NC3 4.4 40.9 1.0
OE1 O:GLN477 4.9 27.5 1.0

Reference:

V.M.Purpero, M.P.Valley, D.H.Ohlendorf, J.D.Lipscomb. Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis To Be Published 2010.
Page generated: Tue Aug 5 03:39:38 2025

Last articles

I in 6WXM
I in 6X42
I in 6X2D
I in 6WYQ
I in 6WOK
I in 6WNY
I in 6W9D
I in 6WC8
I in 6WE7
I in 6W35
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy