Iron in PDB 1dmj: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine, PDB code: 1dmj was solved by P.Kotsonis, L.G.Frohlich, C.S.Raman, H.Li, M.Berg, R.Gerwig, V.Groehn, Y.Kang, N.Al-Masoudi, S.Taghavi-Moghadam, D.Mohr, U.Munch, J.Schnabel, P.Martasek, B.S.Masters, H.Strobel, T.Poulos, H.Matter, W.Pfleiderer, H.H.Schmidt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.38 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.900, 106.490, 156.550, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 22.8

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine (pdb code 1dmj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine, PDB code: 1dmj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:20.4 occ:1.00 FE A:HEM1500 0.0 20.4 1.0 ND A:HEM1500 2.0 18.5 1.0 NB A:HEM1500 2.0 17.8 1.0 NA A:HEM1500 2.0 20.0 1.0 NC A:HEM1500 2.0 19.3 1.0 SG A:CYS186 2.2 18.6 1.0 C4D A:HEM1500 3.0 20.5 1.0 C1D A:HEM1500 3.1 20.8 1.0 C1A A:HEM1500 3.1 19.3 1.0 C1B A:HEM1500 3.1 19.2 1.0 C4C A:HEM1500 3.1 18.5 1.0 C4B A:HEM1500 3.1 20.2 1.0 C1C A:HEM1500 3.1 17.9 1.0 C4A A:HEM1500 3.1 18.8 1.0 CB A:CYS186 3.3 19.7 1.0 CHA A:HEM1500 3.4 18.1 1.0 CHD A:HEM1500 3.4 20.6 1.0 CHB A:HEM1500 3.5 18.7 1.0 CHC A:HEM1500 3.5 19.7 1.0 C2 A:ITU1800 3.8 21.7 1.0 S A:ITU1800 4.0 23.9 1.0 CA A:CYS186 4.1 17.4 1.0 C2D A:HEM1500 4.3 20.4 1.0 C3D A:HEM1500 4.3 20.4 1.0 C2A A:HEM1500 4.3 18.0 1.0 C2B A:HEM1500 4.3 20.1 1.0 C3A A:HEM1500 4.3 17.8 1.0 C3C A:HEM1500 4.3 18.0 1.0 C2C A:HEM1500 4.3 17.1 1.0 C3B A:HEM1500 4.3 20.6 1.0 NE1 A:TRP180 4.4 17.9 1.0 C3 A:ITU1800 4.5 24.1 1.0 N1 A:ITU1800 4.6 23.6 1.0 N A:GLY188 4.8 18.6 1.0 C A:CYS186 4.8 18.8 1.0 N A:VAL187 4.9 16.8 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 5, 6-Cyclic-Tetrahydropteridine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2500 b:22.0 occ:1.00 FE B:HEM2500 0.0 22.0 1.0 ND B:HEM2500 2.0 22.4 1.0 NA B:HEM2500 2.0 22.4 1.0 NC B:HEM2500 2.0 21.0 1.0 NB B:HEM2500 2.0 19.5 1.0 SG B:CYS186 2.3 22.1 1.0 C4D B:HEM2500 3.0 22.1 1.0 C1D B:HEM2500 3.0 23.4 1.0 C1A B:HEM2500 3.1 21.6 1.0 C1B B:HEM2500 3.1 20.6 1.0 C4C B:HEM2500 3.1 21.7 1.0 C1C B:HEM2500 3.1 22.6 1.0 C4A B:HEM2500 3.1 21.5 1.0 C4B B:HEM2500 3.1 22.2 1.0 CB B:CYS186 3.4 21.6 1.0 CHA B:HEM2500 3.4 20.8 1.0 CHD B:HEM2500 3.4 24.7 1.0 CHC B:HEM2500 3.5 21.5 1.0 CHB B:HEM2500 3.5 21.5 1.0 S B:ITU2800 3.9 23.6 1.0 C2 B:ITU2800 4.0 18.7 1.0 CA B:CYS186 4.0 20.5 1.0 C3D B:HEM2500 4.2 23.6 1.0 C2D B:HEM2500 4.3 25.3 1.0 C2A B:HEM2500 4.3 23.0 1.0 NE1 B:TRP180 4.3 19.9 1.0 C2B B:HEM2500 4.3 21.6 1.0 C3A B:HEM2500 4.3 20.7 1.0 C2C B:HEM2500 4.3 23.5 1.0 C3C B:HEM2500 4.3 24.1 1.0 C3B B:HEM2500 4.4 22.2 1.0 C3 B:ITU2800 4.5 22.0 1.0 N1 B:ITU2800 4.6 21.7 1.0 C B:CYS186 4.8 18.9 1.0 N B:GLY188 4.8 21.0 1.0 O B:HOH2915 4.8 27.5 1.0 N B:VAL187 4.9 20.4 1.0 CD1 B:TRP180 5.0 20.3 1.0

P.Kotsonis, L.G.Frohlich, C.S.Raman, H.Li, M.Berg, R.Gerwig, V.Groehn, Y.Kang, N.Al-Masoudi, S.Taghavi-Moghadam, D.Mohr, U.Munch, J.Schnabel, P.Martasek, B.S.Masters, H.Strobel, T.Poulos, H.Matter, W.Pfleiderer, H.H.Schmidt. Structural Basis For Pterin Antagonism in Nitric-Oxide Synthase. Development of Novel 4-Oxo-Pteridine Antagonists of (6R)-5,6,7,8-Tetrahydrobiopterin J.Biol.Chem. V. 276 49133 2001.
ISSN: ISSN 0021-9258
PubMed: 11590164
DOI: 10.1074/JBC.M011469200