Iron in PDB 6bdd: Crystal Structure of Fe(II) Unliganded H-Nox Protein From K. Algicida

The structure of Crystal Structure of Fe(II) Unliganded H-Nox Protein From K. Algicida, PDB code: 6bdd was solved by J.J.Bruegger, C.W.Hespen, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.17 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.966, 57.613, 68.796, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.2

The binding sites of Iron atom in the Crystal Structure of Fe(II) Unliganded H-Nox Protein From K. Algicida (pdb code 6bdd). 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 Crystal Structure of Fe(II) Unliganded H-Nox Protein From K. Algicida, PDB code: 6bdd:

Iron binding site 1 out of 1 in the Crystal Structure of Fe(II) Unliganded H-Nox Protein From K. Algicida


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 Fe(II) Unliganded H-Nox Protein From K. Algicida within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:30.4 occ:1.00 FE A:HEM201 0.0 30.4 1.0 NC A:HEM201 2.0 32.0 1.0 NB A:HEM201 2.0 32.8 1.0 NA A:HEM201 2.0 28.2 1.0 NE2 A:HIS104 2.0 35.2 1.0 ND A:HEM201 2.0 32.0 1.0 CE1 A:HIS104 2.8 30.4 1.0 C4C A:HEM201 3.0 26.8 1.0 C1D A:HEM201 3.0 30.7 1.0 C4A A:HEM201 3.0 30.2 1.0 C1B A:HEM201 3.0 34.2 1.0 C1A A:HEM201 3.1 30.3 1.0 C4B A:HEM201 3.1 30.6 1.0 C1C A:HEM201 3.1 31.2 1.0 C4D A:HEM201 3.1 25.4 1.0 CD2 A:HIS104 3.1 32.1 1.0 CHD A:HEM201 3.4 30.2 1.0 CHB A:HEM201 3.4 37.8 1.0 CHA A:HEM201 3.5 25.0 1.0 CHC A:HEM201 3.5 32.6 1.0 ND1 A:HIS104 4.0 30.2 1.0 CG A:HIS104 4.2 35.3 1.0 C2D A:HEM201 4.2 27.4 1.0 C3C A:HEM201 4.2 27.2 1.0 C3A A:HEM201 4.3 31.7 1.0 C3D A:HEM201 4.3 25.8 1.0 C2B A:HEM201 4.3 35.8 1.0 C2A A:HEM201 4.3 34.1 1.0 C2C A:HEM201 4.3 23.9 1.0 C3B A:HEM201 4.3 33.9 1.0 CD1 A:LEU146 4.3 29.6 1.0 CD2 A:LEU116 4.8 32.5 1.0

C.W.Hespen, J.J.Bruegger, Y.Guo, M.A.Marletta. Native Alanine Substitution in the Glycine Hinge Modulates Conformational Flexibility of Heme Nitric Oxide/Oxygen (H-Nox) Sensing Proteins. Acs Chem. Biol. V. 13 1631 2018.
ISSN: ESSN 1554-8937
PubMed: 29757599
DOI: 10.1021/ACSCHEMBIO.8B00248