Atomistry » Fluorine » PDB 3jx3-3kql » 3kk6
Atomistry »
  Fluorine »
    PDB 3jx3-3kql »
      3kk6 »

Fluorine in PDB 3kk6: Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib

Enzymatic activity of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib

All present enzymatic activity of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib:
1.14.99.1;

Protein crystallography data

The structure of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib, PDB code: 3kk6 was solved by R.S.Sidhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.42 / 2.75
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 181.035, 181.035, 102.698, 90.00, 90.00, 120.00
R / Rfree (%) 20.7 / 24.2

Other elements in 3kk6:

The structure of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib (pdb code 3kk6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib, PDB code: 3kk6:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 1 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F701

b:99.3
occ:1.00
 F3 A:CEL701 0.0 99.3 1.0
C4 A:CEL701 1.3 92.8 1.0
F1 A:CEL701 2.1 92.3 1.0
F2 A:CEL701 2.2 90.1 1.0
C1 A:CEL701 2.3 83.8 1.0
HG11 A:VAL349 2.7 81.4 0.0
HC2 A:CEL701 2.9 77.3 0.0
HD22 A:LEU359 2.9 29.4 0.0
C2 A:CEL701 2.9 73.2 1.0
HD12 A:LEU359 2.9 29.4 0.0
HD21 A:LEU531 3.1 76.5 0.0
HD21 A:LEU359 3.4 29.4 0.0
HD13 A:LEU359 3.4 29.4 0.0
HG12 A:VAL349 3.4 81.4 0.0
HG11 A:VAL116 3.4 28.1 0.0
CG1 A:VAL349 3.5 81.4 1.0
N1 A:CEL701 3.5 79.6 1.0
CD2 A:LEU359 3.5 65.7 1.0
CD1 A:LEU359 3.5 61.6 1.0
HD11 A:LEU531 3.7 76.5 0.0
CD2 A:LEU531 4.0 54.4 1.0
HG13 A:VAL349 4.1 81.4 0.0
CG A:LEU359 4.1 51.7 1.0
C3 A:CEL701 4.2 66.7 1.0
CG1 A:VAL116 4.2 46.1 1.0
HB A:VAL349 4.3 81.4 0.0
HG12 A:VAL116 4.3 28.1 0.0
HD23 A:LEU359 4.3 29.4 0.0
HD11 A:LEU359 4.4 29.4 0.0
HD22 A:LEU531 4.4 76.5 0.0
N2 A:CEL701 4.4 78.5 1.0
HB3 A:LEU359 4.5 29.4 0.0
CB A:VAL349 4.5 78.9 1.0
HD23 A:LEU531 4.5 76.5 0.0
CD1 A:LEU531 4.5 60.6 1.0
HG13 A:VAL116 4.6 28.1 0.0
HG21 A:VAL349 4.6 81.4 0.0
HG A:LEU531 4.6 76.5 0.0
CG A:LEU531 4.7 65.0 1.0
HD13 A:LEU531 4.9 76.5 0.0
HG A:LEU359 4.9 29.4 0.0
CB A:LEU359 4.9 53.5 1.0
H10C A:CEL701 4.9 77.3 0.0
HE2 A:MET113 5.0 43.0 0.0

Fluorine binding site 2 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 2 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F701

b:90.1
occ:1.00
 F2 A:CEL701 0.0 90.1 1.0
C4 A:CEL701 1.3 92.8 1.0
F1 A:CEL701 2.1 92.3 1.0
F3 A:CEL701 2.2 99.3 1.0
C1 A:CEL701 2.3 83.8 1.0
HG11 A:VAL116 2.3 28.1 0.0
HG13 A:VAL116 2.8 28.1 0.0
CG1 A:VAL116 2.9 46.1 1.0
HD11 A:LEU531 2.9 76.5 0.0
C2 A:CEL701 3.0 73.2 1.0
HC2 A:CEL701 3.2 77.3 0.0
HG12 A:VAL116 3.2 28.1 0.0
N1 A:CEL701 3.3 79.6 1.0
HD21 A:LEU531 3.8 76.5 0.0
CD1 A:LEU531 3.9 60.6 1.0
HB1 A:ALA527 4.0 3.3 0.0
HE A:ARG120 4.0 65.6 0.0
HD22 A:LEU359 4.1 29.4 0.0
HG21 A:VAL116 4.1 28.1 0.0
HG3 A:ARG120 4.1 65.6 0.0
HD21 A:LEU359 4.2 29.4 0.0
HD13 A:LEU531 4.2 76.5 0.0
C3 A:CEL701 4.2 66.7 1.0
CB A:VAL116 4.3 63.0 1.0
N2 A:CEL701 4.3 78.5 1.0
HD12 A:LEU531 4.3 76.5 0.0
HG11 A:VAL349 4.4 81.4 0.0
HE2 A:TYR355 4.5 20.4 0.0
HG22 A:VAL116 4.5 28.1 0.0
CG2 A:VAL116 4.5 74.3 1.0
HH21 A:ARG120 4.6 65.6 0.0
NE A:ARG120 4.6 0.6 1.0
HB A:VAL116 4.6 28.1 0.0
CD2 A:LEU531 4.6 54.4 1.0
CD2 A:LEU359 4.6 65.7 1.0
CG A:LEU531 4.7 65.0 1.0
HG A:LEU531 4.7 76.5 0.0
CB A:ALA527 4.8 78.9 1.0
HB2 A:ALA527 4.8 3.3 0.0
HD22 A:LEU531 4.9 76.5 0.0
HD12 A:LEU359 4.9 29.4 0.0
HD13 A:LEU359 5.0 29.4 0.0
HG12 A:VAL349 5.0 81.4 0.0
NH2 A:ARG120 5.0 0.9 1.0

Fluorine binding site 3 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 3 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F701

b:92.3
occ:1.00
 F1 A:CEL701 0.0 92.3 1.0
C4 A:CEL701 1.3 92.8 1.0
F3 A:CEL701 2.1 99.3 1.0
F2 A:CEL701 2.1 90.1 1.0
C1 A:CEL701 2.3 83.8 1.0
HD21 A:LEU359 2.3 29.4 0.0
N1 A:CEL701 2.7 79.6 1.0
HD22 A:LEU359 2.9 29.4 0.0
CD2 A:LEU359 3.0 65.7 1.0
HD13 A:LEU359 3.2 29.4 0.0
HD2 A:TYR355 3.4 20.4 0.0
HG11 A:VAL116 3.4 28.1 0.0
C2 A:CEL701 3.5 73.2 1.0
HD12 A:LEU359 3.6 29.4 0.0
HD23 A:LEU359 3.7 29.4 0.0
CD1 A:LEU359 3.7 61.6 1.0
HE2 A:TYR355 3.8 20.4 0.0
HG12 A:VAL349 3.8 81.4 0.0
HG11 A:VAL349 3.9 81.4 0.0
CG A:LEU359 4.0 51.7 1.0
CD2 A:TYR355 4.0 59.2 1.0
HC2 A:CEL701 4.1 77.3 0.0
N2 A:CEL701 4.1 78.5 1.0
CE2 A:TYR355 4.2 63.6 1.0
HB2 A:SER353 4.3 7.7 0.0
CG1 A:VAL349 4.3 81.4 1.0
CG1 A:VAL116 4.3 46.1 1.0
HG21 A:VAL116 4.4 28.1 0.0
HG A:LEU359 4.4 29.4 0.0
C3 A:CEL701 4.4 66.7 1.0
HG13 A:VAL116 4.5 28.1 0.0
CB A:SER353 4.6 65.8 1.0
HD11 A:LEU359 4.6 29.4 0.0
HG13 A:VAL349 4.8 81.4 0.0
H17C A:CEL701 4.8 77.3 0.0
HG12 A:VAL116 4.8 28.1 0.0
HG A:SER353 4.9 7.7 0.0
HD11 A:LEU531 4.9 76.5 0.0
OG A:SER353 4.9 71.3 1.0
HB2 A:TYR355 4.9 20.4 0.0

Fluorine binding site 4 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 4 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1701

b:58.3
occ:0.50
 F3 B:CEL1701 0.0 58.3 0.5
C4 B:CEL1701 1.3 50.6 0.5
F1 B:CEL1701 2.1 66.5 0.5
F2 B:CEL1701 2.2 55.4 0.5
C1 B:CEL1701 2.3 34.1 0.5
HG11 B:VAL349 2.8 48.7 0.0
HC2 B:CEL1701 2.9 65.8 0.0
HD22 B:LEU359 2.9 70.6 0.0
C2 B:CEL1701 2.9 29.2 0.5
HD13 B:LEU359 2.9 70.6 0.0
HD21 B:LEU531 3.1 71.8 0.0
HD21 B:LEU359 3.4 70.6 0.0
HD11 B:LEU359 3.4 70.6 0.0
HG12 B:VAL349 3.4 48.7 0.0
HG11 B:VAL116 3.4 28.7 0.0
N1 B:CEL1701 3.5 37.8 0.5
CD2 B:LEU359 3.5 70.0 1.0
CG1 B:VAL349 3.5 82.7 1.0
CD1 B:LEU359 3.5 64.2 1.0
HD11 B:LEU531 3.7 71.8 0.0
CD2 B:LEU531 4.0 51.1 1.0
HG13 B:VAL349 4.1 48.7 0.0
CG B:LEU359 4.1 55.2 1.0
C3 B:CEL1701 4.2 30.9 0.5
CG1 B:VAL116 4.2 44.4 1.0
HG12 B:VAL116 4.3 28.7 0.0
HD23 B:LEU359 4.3 70.6 0.0
HD12 B:LEU359 4.4 70.6 0.0
HD22 B:LEU531 4.4 71.8 0.0
HB B:VAL349 4.4 48.7 0.0
N2 B:CEL1701 4.4 45.9 0.5
HB3 B:LEU359 4.5 70.6 0.0
HD23 B:LEU531 4.5 71.8 0.0
CD1 B:LEU531 4.5 57.3 1.0
CB B:VAL349 4.5 75.6 1.0
HG21 B:VAL349 4.6 48.7 0.0
HE2 B:TYR355 4.6 90.7 0.0
HG13 B:VAL116 4.6 28.7 0.0
HG B:LEU531 4.6 71.8 0.0
CG B:LEU531 4.7 61.8 1.0
HB3 B:SER353 4.8 0.8 0.0
HD13 B:LEU531 4.9 71.8 0.0
HG B:LEU359 4.9 70.6 0.0
CB B:LEU359 4.9 56.4 1.0
H10C B:CEL1701 4.9 65.8 0.0
HE1 B:MET113 5.0 0.0 0.0

Fluorine binding site 5 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 5 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1701

b:55.4
occ:0.50
 F2 B:CEL1701 0.0 55.4 0.5
C4 B:CEL1701 1.3 50.6 0.5
F1 B:CEL1701 2.1 66.5 0.5
F3 B:CEL1701 2.2 58.3 0.5
HG11 B:VAL116 2.3 28.7 0.0
C1 B:CEL1701 2.3 34.1 0.5
HG13 B:VAL116 2.8 28.7 0.0
CG1 B:VAL116 2.9 44.4 1.0
HD11 B:LEU531 2.9 71.8 0.0
C2 B:CEL1701 3.0 29.2 0.5
HC2 B:CEL1701 3.2 65.8 0.0
HG12 B:VAL116 3.2 28.7 0.0
N1 B:CEL1701 3.3 37.8 0.5
HE2 B:TYR355 3.8 90.7 0.0
HD21 B:LEU531 3.8 71.8 0.0
CD1 B:LEU531 3.9 57.3 1.0
HB1 B:ALA527 4.0 0.7 0.0
HD22 B:LEU359 4.1 70.6 0.0
HG21 B:VAL116 4.1 28.7 0.0
HE B:ARG120 4.1 80.7 0.0
HE B:ARG120 4.2 80.7 0.0
HD13 B:LEU531 4.2 71.8 0.0
HD21 B:LEU359 4.2 70.6 0.0
C3 B:CEL1701 4.2 30.9 0.5
CB B:VAL116 4.2 63.8 1.0
N2 B:CEL1701 4.3 45.9 0.5
HG3 B:ARG120 4.3 80.7 0.0
HG3 B:ARG120 4.3 80.7 0.0
HD12 B:LEU531 4.3 71.8 0.0
HH21 B:ARG120 4.4 80.7 0.0
HH21 B:ARG120 4.5 80.7 0.0
HG11 B:VAL349 4.5 48.7 0.0
HG22 B:VAL116 4.5 28.7 0.0
CG2 B:VAL116 4.5 70.2 1.0
HB B:VAL116 4.6 28.7 0.0
CD2 B:LEU531 4.6 51.1 1.0
CD2 B:LEU359 4.6 70.0 1.0
CE2 B:TYR355 4.7 67.9 1.0
CG B:LEU531 4.7 61.8 1.0
HG B:LEU531 4.7 71.8 0.0
NE B:ARG120 4.7 81.3 0.5
NE B:ARG120 4.8 81.4 0.5
CB B:ALA527 4.8 79.9 1.0
HB2 B:ALA527 4.9 0.7 0.0
HD22 B:LEU531 4.9 71.8 0.0
HD13 B:LEU359 4.9 70.6 0.0
HD11 B:LEU359 5.0 70.6 0.0

Fluorine binding site 6 out of 6 in 3kk6

Go back to Fluorine Binding Sites List in 3kk6
Fluorine binding site 6 out of 6 in the Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Cyclooxygenase-1 in Complex with Celecoxib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1701

b:66.5
occ:0.50
 F1 B:CEL1701 0.0 66.5 0.5
C4 B:CEL1701 1.3 50.6 0.5
F3 B:CEL1701 2.1 58.3 0.5
F2 B:CEL1701 2.1 55.4 0.5
C1 B:CEL1701 2.3 34.1 0.5
HD21 B:LEU359 2.3 70.6 0.0
HE2 B:TYR355 2.6 90.7 0.0
N1 B:CEL1701 2.7 37.8 0.5
HD22 B:LEU359 2.9 70.6 0.0
CD2 B:LEU359 3.0 70.0 1.0
HD2 B:TYR355 3.1 90.7 0.0
HD11 B:LEU359 3.2 70.6 0.0
CE2 B:TYR355 3.4 67.9 1.0
HG11 B:VAL116 3.4 28.7 0.0
C2 B:CEL1701 3.5 29.2 0.5
CD2 B:TYR355 3.6 57.2 1.0
HD13 B:LEU359 3.6 70.6 0.0
HD23 B:LEU359 3.7 70.6 0.0
CD1 B:LEU359 3.7 64.2 1.0
HB3 B:SER353 3.8 0.8 0.0
HG12 B:VAL349 3.8 48.7 0.0
CG B:LEU359 4.0 55.2 1.0
HG11 B:VAL349 4.0 48.7 0.0
HC2 B:CEL1701 4.1 65.8 0.0
N2 B:CEL1701 4.1 45.9 0.5
CG1 B:VAL116 4.3 44.4 1.0
CG1 B:VAL349 4.4 82.7 1.0
HG21 B:VAL116 4.4 28.7 0.0
HG B:LEU359 4.4 70.6 0.0
C3 B:CEL1701 4.4 30.9 0.5
HB2 B:SER353 4.5 0.8 0.0
HG13 B:VAL116 4.5 28.7 0.0
CB B:SER353 4.5 71.6 1.0
CZ B:TYR355 4.6 83.9 1.0
HD12 B:LEU359 4.6 70.6 0.0
HG13 B:VAL349 4.8 48.7 0.0
H17C B:CEL1701 4.8 65.8 0.0
HG12 B:VAL116 4.8 28.7 0.0
HD11 B:LEU531 4.9 71.8 0.0
HG B:SER353 4.9 0.8 0.0
HH B:TYR355 4.9 90.7 0.0
CG B:TYR355 4.9 73.5 1.0
OG B:SER353 5.0 81.4 1.0

Reference:

G.Rimon, R.S.Sidhu, D.A.Lauver, J.Y.Lee, N.P.Sharma, C.Yuan, R.A.Frieler, R.C.Trievel, B.R.Lucchesi, W.L.Smith. Coxibs Interfere with the Action of Aspirin By Binding Tightly to One Monomer of Cyclooxygenase-1. Proc.Natl.Acad.Sci.Usa V. 107 28 2010.
ISSN: ISSN 0027-8424
PubMed: 19955429
DOI: 10.1073/PNAS.0909765106
Page generated: Wed Jul 31 19:55:20 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