Atomistry » Chlorine » PDB 3lcd-3lnr » 3lkt
Atomistry »
  Chlorine »
    PDB 3lcd-3lnr »
      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 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy