Iron in PDB 2fc1: Heme No Complex in Nos

All present enzymatic activity of Heme No Complex in Nos:
1.14.13.39;

The structure of Heme No Complex in Nos, PDB code: 2fc1 was solved by K.Pant, B.R.Crane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.009, 93.517, 62.768, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 26

The binding sites of Iron atom in the Heme No Complex in Nos (pdb code 2fc1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Heme No Complex in Nos, PDB code: 2fc1:

Iron binding site 1 out of 1 in the Heme No Complex in Nos


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Heme No Complex in Nos within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:22.9 occ:1.00 FE A:HEM901 0.0 22.9 1.0 N A:NO902 1.7 32.4 1.0 ND A:HEM901 1.9 21.6 1.0 NA A:HEM901 2.0 20.5 1.0 NC A:HEM901 2.0 21.6 1.0 NB A:HEM901 2.0 20.9 1.0 SG A:CYS62 2.3 42.0 1.0 O A:NO902 2.6 29.2 1.0 C4D A:HEM901 2.9 21.0 1.0 C1D A:HEM901 3.0 14.0 1.0 C4C A:HEM901 3.0 16.3 1.0 C1A A:HEM901 3.0 20.3 1.0 C1B A:HEM901 3.0 15.7 1.0 C4A A:HEM901 3.0 16.9 1.0 C1C A:HEM901 3.0 15.5 1.0 C4B A:HEM901 3.1 15.0 1.0 CB A:CYS62 3.3 37.1 1.0 CHA A:HEM901 3.3 20.7 1.0 CHD A:HEM901 3.3 16.2 1.0 CHB A:HEM901 3.3 17.5 1.0 CHC A:HEM901 3.4 13.2 1.0 CA A:CYS62 4.1 39.8 1.0 C3D A:HEM901 4.2 18.9 1.0 NH1 A:ARG2000 4.2 18.1 1.0 C2A A:HEM901 4.2 21.0 1.0 C2D A:HEM901 4.2 19.3 1.0 C3C A:HEM901 4.2 15.6 1.0 C2B A:HEM901 4.2 16.9 1.0 C3A A:HEM901 4.2 22.6 1.0 C2C A:HEM901 4.2 17.4 1.0 C3B A:HEM901 4.3 19.1 1.0 CZ A:ARG2000 4.5 19.1 1.0 NE1 A:TRP56 4.5 37.8 1.0 NE A:ARG2000 4.9 18.5 1.0 C A:CYS62 5.0 41.4 1.0 CD A:ARG2000 5.0 26.3 1.0 N A:ILE63 5.0 41.7 1.0

K.Pant, B.R.Crane. Nitrosyl-Heme Structures of Bacillus Subtilis Nitric Oxide Synthase Have Implications For Understanding Substrate Oxidation. Biochemistry V. 45 2537 2006.
ISSN: ISSN 0006-2960
PubMed: 16489746
DOI: 10.1021/BI0518848