Iron in PDB 5jrx: Crystal Structure of Fe(II) Co-Bound H-Nox Protein From C. Subterraneus

The structure of Crystal Structure of Fe(II) Co-Bound H-Nox Protein From C. Subterraneus, PDB code: 5jrx was solved by J.Bruegger, C.Hespen, C.M.Phillips-Piro, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.19 / 1.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.865, 127.205, 42.699, 90.00, 95.79, 90.00
R / Rfree (%)	18.6 / 22.5

The binding sites of Iron atom in the Crystal Structure of Fe(II) Co-Bound H-Nox Protein From C. Subterraneus (pdb code 5jrx). 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 Fe(II) Co-Bound H-Nox Protein From C. Subterraneus, PDB code: 5jrx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Fe(II) Co-Bound H-Nox Protein From C. Subterraneus


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) Co-Bound H-Nox Protein From C. Subterraneus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:21.4 occ:1.00 FE A:HEM201 0.0 21.4 1.0 C A:CMO202 1.7 16.5 1.0 ND A:HEM201 2.0 19.4 1.0 NC A:HEM201 2.0 18.8 1.0 NA A:HEM201 2.0 19.2 1.0 NB A:HEM201 2.0 23.7 1.0 NE2 A:HIS102 2.0 24.4 1.0 CE1 A:HIS102 2.9 23.6 1.0 O A:CMO202 2.9 48.5 1.0 C4A A:HEM201 3.0 23.8 1.0 C4D A:HEM201 3.0 18.4 1.0 C1C A:HEM201 3.0 24.7 1.0 C1A A:HEM201 3.0 23.6 1.0 C4B A:HEM201 3.0 24.4 1.0 C1D A:HEM201 3.0 21.4 1.0 C4C A:HEM201 3.0 22.9 1.0 C1B A:HEM201 3.0 22.3 1.0 CD2 A:HIS102 3.1 20.0 1.0 CHC A:HEM201 3.4 22.9 1.0 CHA A:HEM201 3.4 22.6 1.0 CHB A:HEM201 3.4 17.9 1.0 CHD A:HEM201 3.4 19.1 1.0 ND1 A:HIS102 4.0 22.2 1.0 CG A:HIS102 4.2 24.7 1.0 C3A A:HEM201 4.2 23.9 1.0 C2A A:HEM201 4.2 24.9 1.0 C3D A:HEM201 4.2 17.7 1.0 C2D A:HEM201 4.2 18.2 1.0 OH A:TYR140 4.2 26.1 1.0 C2C A:HEM201 4.2 21.2 1.0 C3B A:HEM201 4.2 19.8 1.0 C3C A:HEM201 4.2 22.7 1.0 C2B A:HEM201 4.2 22.3 1.0 CZ A:PHE78 4.5 18.5 1.0 CD1 A:LEU144 4.6 21.8 1.0 CE2 A:PHE78 4.6 23.3 1.0 CE2 A:TYR140 4.7 21.8 1.0 CZ A:TYR140 5.0 21.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Fe(II) Co-Bound H-Nox Protein From C. Subterraneus


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 Fe(II) Co-Bound H-Nox Protein From C. Subterraneus within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:36.2 occ:1.00 FE B:HEM201 0.0 36.2 1.0 C B:CMO202 1.7 29.2 1.0 NC B:HEM201 2.0 34.5 1.0 NA B:HEM201 2.0 39.6 1.0 NE2 B:HIS102 2.0 36.4 1.0 NB B:HEM201 2.0 37.0 1.0 ND B:HEM201 2.0 43.9 1.0 CE1 B:HIS102 2.6 39.2 1.0 O B:CMO202 2.9 55.3 1.0 C1D B:HEM201 2.9 30.8 1.0 C4C B:HEM201 3.0 37.6 1.0 C4A B:HEM201 3.0 48.4 1.0 C1B B:HEM201 3.0 35.1 1.0 C4B B:HEM201 3.1 36.8 1.0 C1A B:HEM201 3.1 48.6 1.0 C4D B:HEM201 3.1 43.7 1.0 C1C B:HEM201 3.1 43.1 1.0 CD2 B:HIS102 3.3 45.7 1.0 CHD B:HEM201 3.3 32.2 1.0 CHB B:HEM201 3.3 37.1 1.0 CHC B:HEM201 3.5 41.1 1.0 CHA B:HEM201 3.5 43.8 1.0 ND1 B:HIS102 3.9 39.5 1.0 OH B:TYR140 4.2 53.9 1.0 C2D B:HEM201 4.2 41.5 1.0 CG B:HIS102 4.2 34.5 1.0 C3A B:HEM201 4.2 46.6 1.0 C3C B:HEM201 4.2 32.7 1.0 C2A B:HEM201 4.3 46.2 1.0 C2B B:HEM201 4.3 39.5 1.0 C3D B:HEM201 4.3 39.1 1.0 C3B B:HEM201 4.3 33.5 1.0 C2C B:HEM201 4.3 33.0 1.0 CZ B:PHE78 4.6 35.1 1.0 CD1 B:LEU144 4.8 30.8 1.0 CE2 B:PHE78 4.8 33.8 1.0 CD1 B:ILE5 4.9 30.8 1.0 CE2 B:TYR140 5.0 35.1 1.0

C.W.Hespen, J.J.Bruegger, C.M.Phillips-Piro, M.A.Marletta. Structural and Functional Evidence Indicates Selective Oxygen Signaling in Caldanaerobacter Subterraneus H-Nox. Acs Chem.Biol. V. 11 2337 2016.
ISSN: ESSN 1554-8937
PubMed: 27328180
DOI: 10.1021/ACSCHEMBIO.6B00431