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

Iron in PDB 3lmx: Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis

Enzymatic activity of Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis

All present enzymatic activity of Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis:
1.13.11.3;

Protein crystallography data

The structure of Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis, PDB code: 3lmx was solved by V.M.Purpero, J.D.Lipscomb, K.Shi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.85 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 127.982, 140.578, 167.824, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 21.3

Other elements in 3lmx:

The structure of Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis also contains other interesting chemical elements:

Chlorine (Cl) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis (pdb code 3lmx). 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 34,-Dioxygenase Controls Efficient Progress Through Catalysis, PDB code: 3lmx:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 3lmx

Go back to Iron Binding Sites List in 3lmx
Iron binding site 1 out of 3 in the Tyrosine 447 of Protocatechuate 34,-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 34,-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Fe600

b:38.0
occ:1.00
O4 M:DHB1 1.8 48.8 0.9
OH M:TYR408 2.0 36.7 1.0
NE2 M:HIS462 2.1 21.5 1.0
NE2 M:HIS460 2.2 26.6 1.0
O3 M:DHB1 2.4 46.1 0.9
C4 M:DHB1 2.7 46.7 0.9
C3 M:DHB1 2.9 44.1 0.9
CZ M:TYR408 3.0 33.8 1.0
CE1 M:HIS462 3.0 19.9 1.0
CD2 M:HIS460 3.1 25.1 1.0
CD2 M:HIS462 3.2 21.3 1.0
CE1 M:HIS460 3.3 27.3 1.0
CE2 M:TYR408 3.6 33.2 1.0
CE1 M:TYR408 3.9 35.1 1.0
C5 M:DHB1 3.9 45.8 0.9
NH1 M:ARG457 4.1 22.8 1.0
ND1 M:HIS462 4.2 21.6 1.0
O A:HOH378 4.2 38.0 1.0
O M:HOH184 4.2 25.2 1.0
C2 M:DHB1 4.2 44.9 0.9
CG M:HIS462 4.3 22.5 1.0
CG M:HIS460 4.3 25.6 1.0
ND1 M:HIS460 4.4 26.1 1.0
OE1 M:GLN477 4.7 28.6 1.0
CD2 M:TYR408 4.9 34.7 1.0
CD2 A:TYR16 5.0 50.3 1.0
C6 M:DHB1 5.0 44.8 0.9

Iron binding site 2 out of 3 in 3lmx

Go back to Iron Binding Sites List in 3lmx
Iron binding site 2 out of 3 in the Tyrosine 447 of Protocatechuate 34,-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 34,-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe600

b:37.2
occ:1.00
O4 N:DHB2 2.0 45.3 0.9
OH N:TYR408 2.0 43.7 1.0
NE2 N:HIS460 2.2 23.3 1.0
NE2 N:HIS462 2.3 26.4 1.0
O3 N:DHB2 2.4 45.4 0.9
C4 N:DHB2 2.8 43.4 0.9
C3 N:DHB2 2.9 43.1 0.9
CZ N:TYR408 3.0 42.1 1.0
CE1 N:HIS462 3.2 26.0 1.0
CD2 N:HIS460 3.2 23.7 1.0
CE1 N:HIS460 3.2 25.3 1.0
CD2 N:HIS462 3.4 24.9 1.0
CE2 N:TYR408 3.7 40.5 1.0
CE1 N:TYR408 3.9 42.1 1.0
NH1 N:ARG457 3.9 23.6 1.0
C5 N:DHB2 4.1 44.6 0.9
O N:HOH34 4.3 25.3 1.0
C2 N:DHB2 4.3 44.2 0.9
O B:HOH219 4.3 32.0 1.0
ND1 N:HIS460 4.3 25.8 1.0
ND1 N:HIS462 4.3 25.9 1.0
CG N:HIS460 4.4 23.8 1.0
CG N:HIS462 4.5 26.3 1.0
OE1 N:GLN477 4.7 28.8 1.0
CD2 N:TYR408 5.0 40.1 1.0

Iron binding site 3 out of 3 in 3lmx

Go back to Iron Binding Sites List in 3lmx
Iron binding site 3 out of 3 in the Tyrosine 447 of Protocatechuate 34,-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 34,-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Fe600

b:37.3
occ:1.00
OH O:TYR408 1.9 41.0 1.0
O4 O:DHB3 2.0 51.0 0.9
O3 O:DHB3 2.2 45.1 0.9
NE2 O:HIS460 2.3 24.7 1.0
NE2 O:HIS462 2.4 25.2 1.0
C4 O:DHB3 2.7 46.7 0.9
C3 O:DHB3 2.8 45.3 0.9
CZ O:TYR408 2.9 38.8 1.0
CE1 O:HIS460 3.2 24.1 1.0
CE1 O:HIS462 3.2 24.9 1.0
CD2 O:HIS460 3.4 26.1 1.0
CD2 O:HIS462 3.4 22.5 1.0
CE2 O:TYR408 3.7 37.2 1.0
CE1 O:TYR408 3.7 37.5 1.0
C5 O:DHB3 4.0 48.2 0.9
O C:HOH324 4.1 34.4 1.0
C2 O:DHB3 4.2 46.6 0.9
NH1 O:ARG457 4.2 23.8 1.0
ND1 O:HIS460 4.3 23.6 1.0
ND1 O:HIS462 4.4 25.3 1.0
O O:HOH167 4.4 27.1 1.0
CG O:HIS460 4.5 25.2 1.0
CG O:HIS462 4.5 25.9 1.0
CD2 C:TYR16 4.6 53.4 1.0
OE1 O:GLN477 4.8 26.4 1.0
CD2 O:TYR408 4.9 38.2 1.0
CD1 O:TYR408 5.0 39.6 1.0

Reference:

V.M.Purpero, J.D.Lipscomb, D.H.Ohlendorf, K.Shi, K.B.Dolbeare, C.K.Brown, D.Burk. Tyrosine 447 of Protocatechuate 34,-Dioxygenase Controls Efficient Progress Through Catalysis To Be Published.
Page generated: Sun Aug 4 14:30:19 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy