Iron in PDB 1dmk: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 4- Amino-6-Phenyl-Tetrahydropteridine

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 4- Amino-6-Phenyl-Tetrahydropteridine:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 4- Amino-6-Phenyl-Tetrahydropteridine, PDB code: 1dmk 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)	19.93 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.070, 106.110, 156.210, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 26.4

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 4- Amino-6-Phenyl-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 4- Amino-6-Phenyl-Tetrahydropteridine (pdb code 1dmk). 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 4- Amino-6-Phenyl-Tetrahydropteridine, PDB code: 1dmk:
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 4- Amino-6-Phenyl-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 4- Amino-6-Phenyl-Tetrahydropteridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:30.8 occ:1.00 FE A:HEM1500 0.0 30.8 1.0 NC A:HEM1500 2.0 26.6 1.0 NB A:HEM1500 2.0 25.7 1.0 NA A:HEM1500 2.0 27.6 1.0 ND A:HEM1500 2.0 26.5 1.0 SG A:CYS186 2.3 30.9 1.0 C1D A:HEM1500 3.0 28.8 1.0 C1B A:HEM1500 3.1 27.6 1.0 C4C A:HEM1500 3.1 29.4 1.0 C1C A:HEM1500 3.1 26.8 1.0 C4B A:HEM1500 3.1 27.6 1.0 C4D A:HEM1500 3.1 28.0 1.0 C1A A:HEM1500 3.1 26.9 1.0 C4A A:HEM1500 3.1 27.4 1.0 CB A:CYS186 3.3 31.6 1.0 CHD A:HEM1500 3.4 28.8 1.0 CHC A:HEM1500 3.4 28.2 1.0 CHB A:HEM1500 3.5 28.5 1.0 CHA A:HEM1500 3.5 27.4 1.0 C2 A:ITU1800 3.8 29.7 1.0 S A:ITU1800 4.0 31.8 1.0 CA A:CYS186 4.0 30.8 1.0 C2D A:HEM1500 4.3 29.7 1.0 C2C A:HEM1500 4.3 28.5 1.0 C3D A:HEM1500 4.3 29.9 1.0 C3C A:HEM1500 4.3 28.4 1.0 C2B A:HEM1500 4.3 27.5 1.0 C2A A:HEM1500 4.3 28.6 1.0 C3B A:HEM1500 4.3 28.6 1.0 C3A A:HEM1500 4.4 28.4 1.0 NE1 A:TRP180 4.4 28.1 1.0 C3 A:ITU1800 4.5 32.5 1.0 N1 A:ITU1800 4.7 31.0 1.0 C A:CYS186 4.8 30.8 1.0 N A:GLY188 4.8 31.6 1.0 N A:VAL187 4.9 31.3 1.0 O A:HOH2050 4.9 47.4 1.0 CD1 A:TRP180 5.0 29.2 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 4- Amino-6-Phenyl-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 4- Amino-6-Phenyl-Tetrahydropteridine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2500 b:28.8 occ:1.00 FE B:HEM2500 0.0 28.8 1.0 ND B:HEM2500 2.0 31.4 1.0 NC B:HEM2500 2.0 32.0 1.0 NA B:HEM2500 2.0 32.1 1.0 NB B:HEM2500 2.0 33.0 1.0 SG B:CYS186 2.3 30.8 1.0 C1D B:HEM2500 3.1 29.6 1.0 C4D B:HEM2500 3.1 31.0 1.0 C4C B:HEM2500 3.1 29.6 1.0 C4A B:HEM2500 3.1 30.4 1.0 C1B B:HEM2500 3.1 32.5 1.0 C1A B:HEM2500 3.1 30.8 1.0 C1C B:HEM2500 3.1 32.3 1.0 C4B B:HEM2500 3.1 33.0 1.0 CB B:CYS186 3.4 32.7 1.0 CHD B:HEM2500 3.4 29.2 1.0 CHB B:HEM2500 3.4 31.2 1.0 CHA B:HEM2500 3.5 30.0 1.0 CHC B:HEM2500 3.5 32.5 1.0 C2 B:ITU2800 4.0 33.6 1.0 S B:ITU2800 4.0 34.6 1.0 CA B:CYS186 4.1 30.7 1.0 NE1 B:TRP180 4.2 37.1 1.0 C3D B:HEM2500 4.3 31.0 1.0 C2D B:HEM2500 4.3 30.6 1.0 C2A B:HEM2500 4.3 31.4 1.0 C3A B:HEM2500 4.3 31.1 1.0 C2B B:HEM2500 4.3 32.8 1.0 C2C B:HEM2500 4.3 31.0 1.0 C3B B:HEM2500 4.3 33.2 1.0 C3C B:HEM2500 4.3 31.1 1.0 C3 B:ITU2800 4.6 32.0 1.0 N1 B:ITU2800 4.7 31.8 1.0 N B:GLY188 4.8 29.9 1.0 C B:CYS186 4.8 29.3 1.0 N B:VAL187 4.9 28.6 1.0 O B:HOH2957 4.9 40.0 1.0 CD1 B:TRP180 4.9 38.1 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