Iron in PDB 1ht5: The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen

All present enzymatic activity of The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen:
1.14.99.1;

The structure of The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen, PDB code: 1ht5 was solved by B.S.Selinsky, K.Gupta, C.T.Sharkey, P.J.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.89 / 2.75
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	98.888, 209.450, 223.013, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 25.2

The structure of The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Iron atom in the The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen (pdb code 1ht5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen, PDB code: 1ht5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:38.1 occ:1.00 FE A:HEM601 0.0 38.1 1.0 NB A:HEM601 2.0 41.2 1.0 NA A:HEM601 2.0 41.8 1.0 ND A:HEM601 2.0 39.3 1.0 NC A:HEM601 2.0 40.0 1.0 NE2 A:HIS388 2.2 29.8 1.0 C4D A:HEM601 3.0 39.4 1.0 C4A A:HEM601 3.0 41.5 1.0 C1A A:HEM601 3.0 41.8 1.0 C1B A:HEM601 3.0 41.6 1.0 C1D A:HEM601 3.0 39.1 1.0 C4C A:HEM601 3.0 39.4 1.0 C4B A:HEM601 3.0 41.1 1.0 C1C A:HEM601 3.0 40.1 1.0 CD2 A:HIS388 3.1 30.9 1.0 CE1 A:HIS388 3.2 32.9 1.0 CHA A:HEM601 3.4 41.0 1.0 CHB A:HEM601 3.4 41.4 1.0 CHD A:HEM601 3.4 37.8 1.0 CHC A:HEM601 3.4 40.3 1.0 C3D A:HEM601 4.3 38.6 1.0 CG A:HIS388 4.3 31.5 1.0 C3A A:HEM601 4.3 42.7 1.0 C2A A:HEM601 4.3 43.8 1.0 C2D A:HEM601 4.3 38.2 1.0 C2B A:HEM601 4.3 43.3 1.0 C3C A:HEM601 4.3 40.1 1.0 C3B A:HEM601 4.3 42.6 1.0 C2C A:HEM601 4.3 40.1 1.0 ND1 A:HIS388 4.3 31.8 1.0 OE1 A:GLN203 4.4 37.6 1.0 NE2 A:HIS207 4.4 35.2 1.0 CE1 A:HIS207 4.6 35.5 1.0 CG1 A:VAL447 4.9 30.6 1.0

Iron binding site 2 out of 2 in the The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The 2.75 Angstrom Resolution Model of Ovine Cox-1 Complexed with Methyl Ester Flurbiprofen within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:40.5 occ:1.00 FE B:HEM601 0.0 40.5 1.0 NB B:HEM601 2.0 40.4 1.0 NA B:HEM601 2.0 42.4 1.0 ND B:HEM601 2.0 40.3 1.0 NC B:HEM601 2.0 40.4 1.0 NE2 B:HIS388 2.4 34.3 1.0 C4D B:HEM601 3.0 40.8 1.0 C4A B:HEM601 3.0 41.6 1.0 C1A B:HEM601 3.0 43.2 1.0 C4B B:HEM601 3.0 41.3 1.0 C1B B:HEM601 3.0 40.9 1.0 C1C B:HEM601 3.0 40.7 1.0 C4C B:HEM601 3.0 39.0 1.0 C1D B:HEM601 3.0 39.6 1.0 CD2 B:HIS388 3.1 34.0 1.0 CHA B:HEM601 3.4 41.7 1.0 CHB B:HEM601 3.4 40.3 1.0 CHC B:HEM601 3.4 41.4 1.0 CHD B:HEM601 3.4 39.3 1.0 CE1 B:HIS388 3.5 33.8 1.0 OE1 B:GLN203 4.2 39.6 1.0 C3A B:HEM601 4.3 43.0 1.0 C3D B:HEM601 4.3 40.6 1.0 C3B B:HEM601 4.3 42.2 1.0 C3C B:HEM601 4.3 39.8 1.0 C2A B:HEM601 4.3 45.2 1.0 C2B B:HEM601 4.3 42.6 1.0 C2C B:HEM601 4.3 40.7 1.0 C2D B:HEM601 4.3 39.1 1.0 CG B:HIS388 4.4 32.7 1.0 NE2 B:HIS207 4.5 36.1 1.0 ND1 B:HIS388 4.5 33.9 1.0 CE1 B:HIS207 4.7 34.5 1.0 CD B:GLN203 4.9 38.0 1.0 CG1 B:VAL447 4.9 33.3 1.0 CG B:GLN203 5.0 35.3 1.0

B.S.Selinsky, K.Gupta, C.T.Sharkey, P.J.Loll. Structural Analysis of Nsaid Binding By Prostaglandin H2 Synthase: Time-Dependent and Time-Independent Inhibitors Elicit Identical Enzyme Conformations. Biochemistry V. 40 5172 2001.
ISSN: ISSN 0006-2960
PubMed: 11318639
DOI: 10.1021/BI010045S