Iron in PDB 1dw2: Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C

The structure of Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C, PDB code: 1dw2 was solved by D.Leys, K.Backers, T.E.Meyer, W.R.Hagen, M.A.Cusanovich, J.J.Vanbeeumen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	83.345, 103.498, 113.660, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 22.9

The binding sites of Iron atom in the Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C (pdb code 1dw2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C, PDB code: 1dw2:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe113 b:27.1 occ:1.00 FE A:HEM113 0.0 27.1 1.0 N A:NO114 1.8 36.2 1.0 NA A:HEM113 2.0 26.6 1.0 NB A:HEM113 2.0 24.0 1.0 NC A:HEM113 2.0 24.5 1.0 ND A:HEM113 2.0 24.1 1.0 NE2 A:HIS47 2.2 25.3 1.0 O A:NO114 2.7 44.5 1.0 C1A A:HEM113 3.0 25.5 1.0 C4A A:HEM113 3.0 26.0 1.0 C4D A:HEM113 3.0 26.1 1.0 C4B A:HEM113 3.0 23.1 1.0 C1C A:HEM113 3.0 23.4 1.0 C1B A:HEM113 3.0 23.5 1.0 C1D A:HEM113 3.0 26.6 1.0 C4C A:HEM113 3.1 25.0 1.0 CE1 A:HIS47 3.1 26.7 1.0 CD2 A:HIS47 3.2 24.8 1.0 CHA A:HEM113 3.4 24.2 1.0 CHB A:HEM113 3.4 23.0 1.0 CHC A:HEM113 3.4 21.7 1.0 CHD A:HEM113 3.4 26.3 1.0 ND2 A:ASN88 4.0 38.5 1.0 C2A A:HEM113 4.2 26.7 1.0 C3A A:HEM113 4.2 26.7 1.0 C3B A:HEM113 4.2 24.7 1.0 C3D A:HEM113 4.2 30.2 1.0 C2C A:HEM113 4.2 25.3 1.0 C3C A:HEM113 4.2 25.9 1.0 C2B A:HEM113 4.3 22.7 1.0 ND1 A:HIS47 4.3 24.3 1.0 C2D A:HEM113 4.3 27.3 1.0 CB A:ASN88 4.3 37.1 1.0 CG A:HIS47 4.3 25.3 1.0 CG A:ASN88 4.7 38.3 1.0

Iron binding site 2 out of 3 in the Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe113 b:27.3 occ:1.00 FE B:HEM113 0.0 27.3 1.0 N B:NO114 1.9 29.6 1.0 NB B:HEM113 2.0 22.1 1.0 ND B:HEM113 2.0 27.2 1.0 NA B:HEM113 2.0 24.4 1.0 NC B:HEM113 2.0 23.6 1.0 NE2 B:HIS47 2.3 24.4 1.0 O B:NO114 2.7 28.4 1.0 C4A B:HEM113 3.0 23.7 1.0 C1B B:HEM113 3.0 21.9 1.0 C1C B:HEM113 3.0 23.2 1.0 C1A B:HEM113 3.0 26.1 1.0 C4B B:HEM113 3.0 21.8 1.0 C4D B:HEM113 3.0 27.7 1.0 C1D B:HEM113 3.1 27.8 1.0 C4C B:HEM113 3.1 24.5 1.0 CD2 B:HIS47 3.1 23.8 1.0 CE1 B:HIS47 3.3 25.5 1.0 CHB B:HEM113 3.4 23.0 1.0 CHA B:HEM113 3.4 26.0 1.0 CHC B:HEM113 3.4 21.2 1.0 CHD B:HEM113 3.5 23.4 1.0 OD1 B:ASN88 4.1 37.6 1.0 C3B B:HEM113 4.2 20.7 1.0 C2B B:HEM113 4.2 21.1 1.0 C3A B:HEM113 4.2 24.7 1.0 C2A B:HEM113 4.2 27.4 1.0 C2C B:HEM113 4.2 24.4 1.0 C3D B:HEM113 4.2 29.5 1.0 C3C B:HEM113 4.3 22.8 1.0 C2D B:HEM113 4.3 28.2 1.0 CG B:HIS47 4.3 25.3 1.0 ND1 B:HIS47 4.3 25.9 1.0 CB B:ASN88 4.7 34.8 1.0 CG B:ASN88 4.8 34.3 1.0

Iron binding site 3 out of 3 in the Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the Nitric Oxide Complex of Reduced Shp, An Oxygen Binding Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe113 b:31.4 occ:1.00 FE C:HEM113 0.0 31.4 1.0 N C:NO114 1.8 37.2 1.0 NA C:HEM113 2.0 29.8 1.0 NB C:HEM113 2.0 29.3 1.0 ND C:HEM113 2.0 33.4 1.0 NC C:HEM113 2.0 31.4 1.0 NE2 C:HIS47 2.2 27.1 1.0 O C:NO114 2.7 37.1 1.0 C4B C:HEM113 3.0 30.0 1.0 C1A C:HEM113 3.0 30.9 1.0 C4A C:HEM113 3.0 29.6 1.0 C4D C:HEM113 3.0 36.1 1.0 C1B C:HEM113 3.0 28.5 1.0 C1C C:HEM113 3.0 29.5 1.0 C1D C:HEM113 3.0 35.9 1.0 C4C C:HEM113 3.1 31.1 1.0 CE1 C:HIS47 3.1 28.4 1.0 CD2 C:HIS47 3.3 27.0 1.0 CHD C:HEM113 3.4 33.0 1.0 CHB C:HEM113 3.4 29.4 1.0 CHA C:HEM113 3.4 32.3 1.0 CHC C:HEM113 3.4 28.8 1.0 C3B C:HEM113 4.2 28.0 1.0 C2A C:HEM113 4.2 32.5 1.0 C3A C:HEM113 4.2 30.1 1.0 C2B C:HEM113 4.2 27.9 1.0 C3C C:HEM113 4.3 30.1 1.0 C2C C:HEM113 4.3 29.6 1.0 C3D C:HEM113 4.3 38.2 1.0 C2D C:HEM113 4.3 37.1 1.0 ND2 C:ASN88 4.3 42.0 1.0 ND1 C:HIS47 4.3 26.2 1.0 CG C:HIS47 4.4 27.5 1.0 CB C:ASN88 4.7 43.5 1.0 CB C:TRP84 4.9 43.4 1.0 CG C:ASN88 4.9 43.7 1.0

D.Leys, K.Backers, T.E.Meyer, W.R.Hagen, M.A.Cusanovich, J.J.Van Beeumen. Crystal Structures of An Oxygen-Binding Cytochrome C From Rhodobacter Sphaeroides. J.Biol.Chem. V. 275 16050 2000.
ISSN: ISSN 0021-9258
PubMed: 10821858
DOI: 10.1074/JBC.275.21.16050