Iron in PDB 1mjt: Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu

All present enzymatic activity of Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu:
1.14.13.39;

The structure of Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu, PDB code: 1mjt was solved by L.E.Bird, J.Ren, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.34 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.780, 115.140, 126.020, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 24.1

The binding sites of Iron atom in the Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu (pdb code 1mjt). 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 Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu, PDB code: 1mjt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu


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 Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:25.4 occ:1.00 FE A:HEM500 0.0 25.4 1.0 ND A:HEM500 2.0 24.2 1.0 NA A:HEM500 2.0 17.7 1.0 NC A:HEM500 2.0 18.0 1.0 NB A:HEM500 2.0 25.7 1.0 SG A:CYS62 2.8 35.8 1.0 C1D A:HEM500 3.0 28.5 1.0 C4D A:HEM500 3.0 21.8 1.0 C4A A:HEM500 3.0 27.5 1.0 C1A A:HEM500 3.0 19.2 1.0 C4C A:HEM500 3.0 30.3 1.0 C1B A:HEM500 3.1 26.7 1.0 C1C A:HEM500 3.1 23.0 1.0 C4B A:HEM500 3.1 14.5 1.0 CHD A:HEM500 3.4 22.9 1.0 CHB A:HEM500 3.4 31.2 1.0 CHA A:HEM500 3.5 18.3 1.0 CHC A:HEM500 3.5 17.7 1.0 CB A:CYS62 3.6 22.3 1.0 C2 A:ITU800 4.0 37.1 1.0 S A:ITU800 4.1 38.7 1.0 CA A:CYS62 4.2 30.5 1.0 C2D A:HEM500 4.3 18.5 1.0 C3D A:HEM500 4.3 19.9 1.0 C2A A:HEM500 4.3 26.5 1.0 C3A A:HEM500 4.3 25.0 1.0 C2B A:HEM500 4.3 32.3 1.0 C3C A:HEM500 4.3 32.9 1.0 C2C A:HEM500 4.3 27.8 1.0 C3B A:HEM500 4.3 33.6 1.0 C3 A:ITU800 4.4 34.3 1.0 NE1 A:TRP56 4.6 16.6 1.0 N1 A:ITU800 4.6 36.8 1.0 C A:CYS62 4.9 30.7 1.0 N A:GLY64 5.0 35.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu


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 Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein, in Complex with Nad+ and Seitu within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:26.6 occ:1.00 FE B:HEM501 0.0 26.6 1.0 NC B:HEM501 2.0 23.2 1.0 NB B:HEM501 2.0 28.1 1.0 NA B:HEM501 2.0 22.6 1.0 ND B:HEM501 2.0 25.5 1.0 SG B:CYS62 2.8 32.7 1.0 C4C B:HEM501 3.0 20.9 1.0 C4A B:HEM501 3.0 25.4 1.0 C1B B:HEM501 3.0 14.6 1.0 C1C B:HEM501 3.0 22.0 1.0 C4B B:HEM501 3.1 22.2 1.0 C1D B:HEM501 3.1 18.3 1.0 C1A B:HEM501 3.1 13.8 1.0 C4D B:HEM501 3.1 24.6 1.0 CB B:CYS62 3.4 25.5 1.0 CHC B:HEM501 3.4 16.2 1.0 CHB B:HEM501 3.4 17.8 1.0 CHD B:HEM501 3.4 13.7 1.0 CHA B:HEM501 3.5 18.0 1.0 C2 B:ITU801 3.8 26.0 1.0 S B:ITU801 3.9 32.8 1.0 CA B:CYS62 4.1 18.2 1.0 C3A B:HEM501 4.3 25.2 1.0 C3C B:HEM501 4.3 19.1 1.0 C2C B:HEM501 4.3 14.9 1.0 C2B B:HEM501 4.3 16.5 1.0 C2A B:HEM501 4.3 19.0 1.0 C3B B:HEM501 4.3 23.2 1.0 C2D B:HEM501 4.3 17.8 1.0 C3D B:HEM501 4.3 25.7 1.0 C3 B:ITU801 4.5 27.4 1.0 NE1 B:TRP56 4.5 22.9 1.0 N1 B:ITU801 4.8 23.7 1.0 C B:CYS62 4.9 19.1 1.0 N B:GLY64 4.9 24.2 1.0 N B:ILE63 5.0 24.9 1.0

L.E.Bird, J.Ren, J.Zhang, N.Foxwell, A.R.Hawkins, I.G.Charles, D.K.Stammers. Crystal Structure of Sanos, A Bacterial Nitric Oxide Synthase Oxygenase Protein From Staphylococcus Aureus Structure V. 10 1687 2002.
ISSN: ISSN 0969-2126
PubMed: 12467576
DOI: 10.1016/S0969-2126(02)00911-5