Atomistry » Chlorine » PDB 3lcc-3lnj » 3lkt
Atomistry »
  Chlorine »
    PDB 3lcc-3lnj »
      3lkt »

Chlorine in PDB 3lkt: 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: 3lkt was solved by J.D.Lipscomb, V.M.Purpero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.57 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 190.310, 168.040, 128.160, 90.00, 132.30, 90.00
R / Rfree (%) 14.8 / 17.3

Other elements in 3lkt:

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

Iron (Fe) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis (pdb code 3lkt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 9 binding sites of Chlorine where determined in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis, PDB code: 3lkt:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Chlorine binding site 1 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 1 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl7

b:39.0
occ:1.00
 O M:HOH2298 2.7 32.3 1.0
O O:HOH38 2.7 20.7 1.0
O M:LYS325 2.7 14.2 1.0
O M:HOH2546 2.8 30.6 1.0
N M:ALA329 3.2 14.9 1.0
CB M:ILE328 3.6 15.6 1.0
CB M:ALA329 3.6 16.4 1.0
C M:LYS325 3.7 13.8 1.0
CA M:THR326 3.8 15.1 1.0
O M:THR326 3.8 15.8 1.0
N M:ILE328 3.9 14.8 1.0
C M:THR326 3.9 14.6 1.0
CA M:ILE328 4.0 15.1 1.0
C M:ILE328 4.0 15.3 1.0
CA M:ALA329 4.1 15.4 1.0
N M:THR326 4.2 13.4 1.0
O M:HOH2680 4.2 40.5 1.0
CG2 M:ILE328 4.3 16.2 1.0
CG1 M:ILE328 4.5 14.0 1.0
N M:SER327 4.6 14.8 1.0
OE1 O:GLN334 4.8 22.7 1.0
C M:SER327 4.8 15.3 1.0
CD1 M:ILE328 4.9 15.9 1.0
O A:HOH376 4.9 20.0 1.0
CA M:LYS325 4.9 14.2 1.0
CB O:ALA335 5.0 16.6 1.0

Chlorine binding site 2 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 2 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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
M:Cl8

b:59.2
occ:1.00
 N M:PHE535 3.0 19.0 1.0
CA M:HIS534 3.7 18.8 1.0
O M:HOH1787 3.8 31.0 1.0
C M:HIS534 3.8 18.8 1.0
CA M:PHE535 3.8 19.7 1.0
CB M:HIS534 4.3 18.6 1.0
CG M:PHE535 4.5 19.6 1.0
CD1 M:PHE535 4.6 20.4 1.0
O M:THR533 4.7 19.2 1.0
CB M:PHE535 4.8 19.4 1.0
N M:HIS534 4.8 18.3 1.0
CD2 M:PHE535 4.9 18.5 1.0

Chlorine binding site 3 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 3 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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
M:Cl9

b:45.4
occ:1.00
 O M:HOH931 2.9 24.7 1.0
N M:LEU430 3.1 16.2 1.0
O M:HOH832 3.3 19.9 1.0
O M:HOH1485 3.6 27.3 1.0
CA M:CYS429 3.7 16.9 1.0
CB M:CYS429 3.7 17.4 1.0
C M:CYS429 3.8 16.8 1.0
O M:LEU430 4.0 17.6 1.0
CB M:LEU430 4.0 17.6 1.0
CA M:LEU430 4.0 15.8 1.0
CG M:PHE356 4.4 20.4 1.0
CD1 M:PHE356 4.4 19.3 1.0
CG M:LEU430 4.4 18.5 1.0
O M:HOH1882 4.4 35.5 1.0
CD2 M:PHE356 4.4 20.5 1.0
C M:LEU430 4.5 16.8 1.0
CE1 M:PHE356 4.5 18.5 1.0
CE2 M:PHE356 4.6 19.6 1.0
CZ M:PHE356 4.6 20.2 1.0
O M:HOH1942 4.7 37.7 1.0
O M:HOH837 4.9 20.2 1.0
O M:HOH1049 4.9 24.1 1.0
O M:HOH1098 4.9 24.8 1.0
CB M:PHE356 4.9 20.4 1.0

Chlorine binding site 4 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 4 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 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:Cl14

b:61.9
occ:1.00
 NH2 M:ARG383 3.6 21.9 1.0
NH1 M:ARG383 3.7 24.6 1.0
CZ M:ARG383 4.1 23.8 1.0
O M:HOH1677 4.8 34.0 1.0

Chlorine binding site 5 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 5 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 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:Cl13

b:64.2
occ:1.00
 NH1 N:ARG383 3.7 26.6 1.0
NH2 N:ARG383 3.8 26.0 1.0
CZ N:ARG383 4.2 25.8 1.0

Chlorine binding site 6 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 6 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 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:Cl12

b:70.4
occ:1.00
 NH1 O:ARG383 3.7 25.9 1.0
O O:HOH2447 3.7 42.9 1.0
NH2 O:ARG383 3.7 21.8 1.0
CZ O:ARG383 4.2 24.2 1.0
O O:HOH2043 4.8 37.2 1.0

Chlorine binding site 7 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 7 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Cl15

b:60.1
occ:1.00
 NH1 P:ARG383 3.6 24.4 1.0
NH2 P:ARG383 3.7 20.2 1.0
CZ P:ARG383 4.1 23.6 1.0
O P:HOH2070 4.9 32.6 1.0

Chlorine binding site 8 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 8 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
Q:Cl11

b:68.2
occ:1.00
 NH1 Q:ARG383 3.7 25.9 1.0
NH2 Q:ARG383 3.8 26.6 1.0
CZ Q:ARG383 4.2 25.7 1.0
O Q:HOH2448 4.8 36.9 1.0

Chlorine binding site 9 out of 9 in 3lkt

Go back to Chlorine Binding Sites List in 3lkt
Chlorine binding site 9 out of 9 in the Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Cl10

b:68.4
occ:1.00
 NH2 R:ARG383 3.6 22.0 1.0
NH1 R:ARG383 3.6 25.6 1.0
O R:HOH2449 3.7 41.9 1.0
CZ R:ARG383 4.1 24.2 1.0
NZ N:LYS390 4.3 35.7 1.0
O R:HOH2004 4.8 38.3 1.0

Reference:

V.M.Purpero, M.P.Valley, D.H.Ohlendorf, J.D.Lipscomb, D.Burk, K.B.Dolbeare, K.C.Brown. Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis To Be Published.
Page generated: Sat Jul 20 23:29:44 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy