Iron in PDB 3b6h: Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil

All present enzymatic activity of Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil:
5.3.99.4;

The structure of Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil, PDB code: 3b6h was solved by Y.-C.Li, C.-W.Chiang, H.-C.Yeh, P.-Y.Hsu, F.G.Whitby, L.-H.Wang, N.-L.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.09 / 1.62
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.762, 106.072, 73.901, 90.00, 91.81, 90.00
R / Rfree (%)	20.3 / 22.8

The binding sites of Iron atom in the Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil (pdb code 3b6h). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil, PDB code: 3b6h:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil


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 Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe600 b:13.2 occ:1.00 FE A:HEM600 0.0 13.2 1.0 NC A:HEM600 2.0 13.0 1.0 NB A:HEM600 2.0 12.4 1.0 NA A:HEM600 2.1 12.1 1.0 ND A:HEM600 2.1 13.6 1.0 OAN A:MXD551 2.2 15.4 1.0 SG A:CYS441 2.4 14.8 1.0 NAC A:MXD551 3.0 17.3 1.0 C1C A:HEM600 3.1 12.6 1.0 C4B A:HEM600 3.1 12.3 1.0 C4C A:HEM600 3.1 13.9 1.0 C1B A:HEM600 3.1 11.8 1.0 C1D A:HEM600 3.1 14.8 1.0 C4A A:HEM600 3.1 11.8 1.0 C1A A:HEM600 3.1 12.6 1.0 C4D A:HEM600 3.1 13.1 1.0 CHD A:HEM600 3.4 14.1 1.0 CHC A:HEM600 3.4 13.0 1.0 CB A:CYS441 3.4 14.3 1.0 CHB A:HEM600 3.4 12.2 1.0 CHA A:HEM600 3.5 13.2 1.0 CAA A:MXD551 3.7 16.9 1.0 CAE A:MXD551 3.8 17.8 1.0 NAM A:MXD551 3.8 19.0 1.0 NAO A:MXD551 3.9 18.6 1.0 CA A:CYS441 3.9 14.8 1.0 O A:HOH713 4.2 13.9 1.0 C2C A:HEM600 4.3 13.2 1.0 C3C A:HEM600 4.3 13.9 1.0 C3B A:HEM600 4.3 12.7 1.0 C2B A:HEM600 4.3 11.7 1.0 C3A A:HEM600 4.3 12.4 1.0 C2A A:HEM600 4.3 12.2 1.0 C2D A:HEM600 4.3 15.4 1.0 C3D A:HEM600 4.3 15.0 1.0 N A:LEU442 4.6 14.7 1.0 C A:CYS441 4.7 15.0 1.0 N A:GLY443 4.8 14.8 1.0 NAB A:MXD551 4.9 18.9 1.0 CAF A:MXD551 4.9 19.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil


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 Human Prostacyclin Synthase in Complex with Inhibitor Minoxidil within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:13.2 occ:1.00 FE B:HEM600 0.0 13.2 1.0 NC B:HEM600 2.0 13.0 1.0 NA B:HEM600 2.0 13.5 1.0 NB B:HEM600 2.1 13.0 1.0 ND B:HEM600 2.1 13.8 1.0 OAN B:MXD551 2.2 16.4 1.0 SG B:CYS441 2.4 13.9 1.0 NAC B:MXD551 3.0 18.6 1.0 C4C B:HEM600 3.1 14.2 1.0 C1C B:HEM600 3.1 13.1 1.0 C1A B:HEM600 3.1 14.1 1.0 C1D B:HEM600 3.1 14.8 1.0 C1B B:HEM600 3.1 12.4 1.0 C4A B:HEM600 3.1 13.0 1.0 C4D B:HEM600 3.1 14.8 1.0 C4B B:HEM600 3.1 12.6 1.0 CB B:CYS441 3.4 13.6 1.0 CHD B:HEM600 3.4 14.4 1.0 CHC B:HEM600 3.4 14.3 1.0 CHB B:HEM600 3.4 13.5 1.0 CHA B:HEM600 3.4 14.9 1.0 CAA B:MXD551 3.8 18.4 1.0 CAE B:MXD551 3.8 18.6 1.0 NAO B:MXD551 3.8 19.1 1.0 NAM B:MXD551 3.8 19.9 1.0 CA B:CYS441 3.9 14.1 1.0 O B:HOH709 4.2 14.8 1.0 C2C B:HEM600 4.3 14.1 1.0 C3C B:HEM600 4.3 14.6 1.0 C2B B:HEM600 4.3 14.0 1.0 C2A B:HEM600 4.3 14.4 1.0 C3A B:HEM600 4.3 14.3 1.0 C3B B:HEM600 4.3 13.5 1.0 C2D B:HEM600 4.3 16.6 1.0 C3D B:HEM600 4.3 15.8 1.0 C B:CYS441 4.7 14.3 1.0 N B:GLY443 4.7 13.6 1.0 N B:LEU442 4.7 14.1 1.0 NAB B:MXD551 4.9 19.5 1.0 CAF B:MXD551 4.9 19.9 1.0

Y.-C.Li, C.-W.Chiang, H.-C.Yeh, P.-Y.Hsu, F.G.Whitby, L.-H.Wang, N.-L.Chan. Structures of Prostacyclin Synthase and Its Complexes with Substrate Analog and Inhibitor Reveal A Ligand-Specific Heme Conformation Change J.Biol.Chem. V. 283 2917 2008.
ISSN: ISSN 0021-9258
PubMed: 18032380
DOI: 10.1074/JBC.M707470200