Atomistry » Iron » PDB 1phb-1q5d » 1pxx
Atomistry »
  Iron »
    PDB 1phb-1q5d »
      1pxx »

Iron in PDB 1pxx: Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2

Enzymatic activity of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2

All present enzymatic activity of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2:
1.14.99.1;

Protein crystallography data

The structure of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2, PDB code: 1pxx was solved by J.R.Kiefer, S.W.Rowlinson, J.J.Prusakiewicz, J.L.Pawlitz, K.R.Kozak, A.S.Kalgutkar, W.C.Stallings, L.J.Marnett, R.G.Kurumbail, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 181.145, 135.090, 124.165, 90.00, 90.00, 90.00
R / Rfree (%) 25.4 / 30.2

Other elements in 1pxx:

The structure of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 also contains other interesting chemical elements:

Chlorine (Cl) 8 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 (pdb code 1pxx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2, PDB code: 1pxx:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1pxx

Go back to Iron Binding Sites List in 1pxx
Iron binding site 1 out of 4 in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe704

b:18.8
occ:1.00
FE A:HEM704 0.0 18.8 1.0
ND A:HEM704 1.9 15.6 1.0
NA A:HEM704 2.0 18.3 1.0
NC A:HEM704 2.0 11.1 1.0
NB A:HEM704 2.0 14.0 1.0
NE2 A:HIS388 2.2 17.7 1.0
C1D A:HEM704 3.0 15.4 1.0
C4D A:HEM704 3.0 16.7 1.0
C4C A:HEM704 3.0 9.9 1.0
C1A A:HEM704 3.0 22.0 1.0
C4A A:HEM704 3.0 16.4 1.0
C1C A:HEM704 3.0 9.1 1.0
C1B A:HEM704 3.0 13.6 1.0
C4B A:HEM704 3.0 12.4 1.0
CD2 A:HIS388 3.2 19.4 1.0
CE1 A:HIS388 3.2 17.9 1.0
CHD A:HEM704 3.4 13.8 1.0
CHA A:HEM704 3.4 17.9 1.0
CHB A:HEM704 3.4 13.9 1.0
CHC A:HEM704 3.4 9.9 1.0
C2D A:HEM704 4.2 16.2 1.0
C3D A:HEM704 4.2 17.6 1.0
C3A A:HEM704 4.2 20.4 1.0
C2A A:HEM704 4.2 24.6 1.0
C3C A:HEM704 4.3 7.0 1.0
C2C A:HEM704 4.3 8.1 1.0
CG A:HIS388 4.3 20.2 1.0
C2B A:HEM704 4.3 10.3 1.0
C3B A:HEM704 4.3 11.4 1.0
ND1 A:HIS388 4.3 20.2 1.0
NE2 A:HIS207 4.5 28.1 1.0
OE1 A:GLN203 4.5 14.4 1.0
CE1 A:HIS207 4.7 27.2 1.0
CG1 A:VAL447 4.9 19.4 1.0

Iron binding site 2 out of 4 in 1pxx

Go back to Iron Binding Sites List in 1pxx
Iron binding site 2 out of 4 in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1601

b:22.9
occ:1.00
FE B:HEM1601 0.0 22.9 1.0
NA B:HEM1601 1.9 22.7 1.0
ND B:HEM1601 2.0 23.5 1.0
NB B:HEM1601 2.0 22.9 1.0
NC B:HEM1601 2.0 18.0 1.0
NE2 B:HIS1388 2.2 18.3 1.0
C1A B:HEM1601 3.0 27.3 1.0
C4D B:HEM1601 3.0 23.7 1.0
C4A B:HEM1601 3.0 25.6 1.0
C1B B:HEM1601 3.0 22.1 1.0
C1D B:HEM1601 3.0 23.4 1.0
C1C B:HEM1601 3.0 17.8 1.0
C4B B:HEM1601 3.0 18.8 1.0
C4C B:HEM1601 3.0 15.9 1.0
CD2 B:HIS1388 3.2 17.6 1.0
CE1 B:HIS1388 3.2 17.3 1.0
O B:HOH5098 3.3 30.0 1.0
CHA B:HEM1601 3.4 27.2 1.0
CHB B:HEM1601 3.4 23.3 1.0
CHC B:HEM1601 3.4 16.0 1.0
CHD B:HEM1601 3.4 18.2 1.0
C3D B:HEM1601 4.2 22.1 1.0
C3A B:HEM1601 4.2 27.7 1.0
C2A B:HEM1601 4.2 31.5 1.0
C2D B:HEM1601 4.3 22.2 1.0
C2B B:HEM1601 4.3 19.8 1.0
C3B B:HEM1601 4.3 19.5 1.0
C2C B:HEM1601 4.3 15.2 1.0
C3C B:HEM1601 4.3 14.1 1.0
CG B:HIS1388 4.3 19.4 1.0
ND1 B:HIS1388 4.3 18.7 1.0
NE2 B:HIS1207 4.4 28.3 1.0
OE1 B:GLN1203 4.5 17.5 1.0
CE1 B:HIS1207 4.6 27.6 1.0
CG1 B:VAL1447 5.0 18.5 1.0

Iron binding site 3 out of 4 in 1pxx

Go back to Iron Binding Sites List in 1pxx
Iron binding site 3 out of 4 in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe2601

b:19.4
occ:1.00
FE C:HEM2601 0.0 19.4 1.0
ND C:HEM2601 2.0 20.4 1.0
NA C:HEM2601 2.0 19.6 1.0
NC C:HEM2601 2.0 16.0 1.0
NB C:HEM2601 2.0 19.9 1.0
NE2 C:HIS2388 2.2 19.1 1.0
C4D C:HEM2601 3.0 22.1 1.0
C1A C:HEM2601 3.0 20.8 1.0
C1D C:HEM2601 3.0 20.6 1.0
C4C C:HEM2601 3.0 15.4 1.0
C4A C:HEM2601 3.0 19.8 1.0
C1C C:HEM2601 3.0 16.3 1.0
C4B C:HEM2601 3.0 17.1 1.0
C1B C:HEM2601 3.0 19.6 1.0
CE1 C:HIS2388 3.1 19.2 1.0
CD2 C:HIS2388 3.2 18.2 1.0
CHA C:HEM2601 3.4 21.6 1.0
CHD C:HEM2601 3.4 18.0 1.0
CHC C:HEM2601 3.4 17.0 1.0
CHB C:HEM2601 3.4 18.4 1.0
C3D C:HEM2601 4.2 23.4 1.0
C2D C:HEM2601 4.2 23.0 1.0
C2A C:HEM2601 4.2 22.5 1.0
C3A C:HEM2601 4.2 18.7 1.0
C3C C:HEM2601 4.3 12.7 1.0
C2C C:HEM2601 4.3 12.3 1.0
C2B C:HEM2601 4.3 20.3 1.0
C3B C:HEM2601 4.3 18.8 1.0
CG C:HIS2388 4.3 19.0 1.0
ND1 C:HIS2388 4.3 19.8 1.0
NE2 C:HIS2207 4.4 28.9 1.0
OE1 C:GLN2203 4.5 15.9 1.0
CE1 C:HIS2207 4.7 27.2 1.0
CG1 C:VAL2447 4.9 18.9 1.0

Iron binding site 4 out of 4 in 1pxx

Go back to Iron Binding Sites List in 1pxx
Iron binding site 4 out of 4 in the Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Diclofenac Bound to the Cyclooxygenase Active Site of Cox-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe3601

b:21.0
occ:1.00
FE D:HEM3601 0.0 21.0 1.0
NA D:HEM3601 1.9 21.5 1.0
ND D:HEM3601 2.0 22.7 1.0
NC D:HEM3601 2.0 16.4 1.0
NB D:HEM3601 2.0 20.7 1.0
NE2 D:HIS3388 2.2 16.5 1.0
C1A D:HEM3601 3.0 26.1 1.0
C4A D:HEM3601 3.0 23.5 1.0
C4D D:HEM3601 3.0 23.5 1.0
C1D D:HEM3601 3.0 20.4 1.0
C1C D:HEM3601 3.0 14.7 1.0
C1B D:HEM3601 3.0 21.9 1.0
C4C D:HEM3601 3.0 13.7 1.0
C4B D:HEM3601 3.0 19.2 1.0
CD2 D:HIS3388 3.1 18.3 1.0
CE1 D:HIS3388 3.1 18.6 1.0
CHA D:HEM3601 3.4 23.8 1.0
CHB D:HEM3601 3.4 21.3 1.0
CHD D:HEM3601 3.4 14.8 1.0
CHC D:HEM3601 3.4 13.3 1.0
C2A D:HEM3601 4.2 29.9 1.0
C3A D:HEM3601 4.2 27.0 1.0
CG D:HIS3388 4.2 19.7 1.0
C3D D:HEM3601 4.2 21.2 1.0
C2C D:HEM3601 4.2 13.3 1.0
C2D D:HEM3601 4.3 19.6 1.0
C3C D:HEM3601 4.3 13.1 1.0
C2B D:HEM3601 4.3 17.7 1.0
ND1 D:HIS3388 4.3 18.9 1.0
C3B D:HEM3601 4.3 19.5 1.0
NE2 D:HIS3207 4.5 27.2 1.0
OE1 D:GLN3203 4.6 16.8 1.0
CE1 D:HIS3207 4.7 27.3 1.0
CG1 D:VAL3447 4.9 19.5 1.0

Reference:

S.W.Rowlinson, J.R.Kiefer, J.J.Prusakiewicz, J.L.Pawlitz, K.R.Kozak, A.S.Kalgutkar, W.C.Stallings, R.G.Kurumbail, L.J.Marnett. A Novel Mechanism of Cyclooxygenase-2 Inhibition Involving Interactions with Ser-530 and Tyr-385. J.Biol.Chem. V. 278 45763 2003.
ISSN: ISSN 0021-9258
PubMed: 12925531
DOI: 10.1074/JBC.M305481200
Page generated: Sat Aug 3 13:14:16 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy