Iron in PDB 2awc: Deoxy-Dcrh-Hr

The structure of Deoxy-Dcrh-Hr, PDB code: 2awc was solved by C.E.Isaza, R.Silaghi-Dumitrescu, R.B.Iyer, D.M.Kurtz, M.K.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.86 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.980, 33.120, 44.700, 90.00, 96.02, 90.00
R / Rfree (%)	20.4 / 25.3

The binding sites of Iron atom in the Deoxy-Dcrh-Hr (pdb code 2awc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Deoxy-Dcrh-Hr, PDB code: 2awc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Deoxy-Dcrh-Hr


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Deoxy-Dcrh-Hr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe137 b:21.6 occ:1.00 FE1 A:FEO137 0.0 21.6 1.0 O A:FEO137 2.0 17.9 1.0 NE2 A:HIS82 2.1 21.1 1.0 NE2 A:HIS118 2.1 25.6 1.0 OD1 A:ASP123 2.2 13.8 1.0 NE2 A:HIS78 2.3 22.1 1.0 OE1 A:GLU63 2.3 24.1 1.0 CE1 A:HIS82 2.9 22.2 1.0 CE1 A:HIS78 3.1 22.1 1.0 CE1 A:HIS118 3.1 21.8 1.0 CD2 A:HIS118 3.1 21.8 1.0 CG A:ASP123 3.2 18.9 1.0 CD A:GLU63 3.2 22.0 1.0 CD2 A:HIS82 3.2 19.4 1.0 OE2 A:GLU63 3.4 20.9 1.0 CD2 A:HIS78 3.4 21.7 1.0 FE2 A:FEO137 3.4 22.1 1.0 OD2 A:ASP123 3.5 15.4 1.0 ND1 A:HIS82 4.1 18.1 1.0 ND1 A:HIS118 4.3 22.5 1.0 CG A:HIS118 4.3 23.4 1.0 CG A:HIS82 4.3 22.1 1.0 ND1 A:HIS78 4.3 18.7 1.0 CG A:HIS78 4.5 22.5 1.0 CB A:ASP123 4.5 18.9 1.0 CG A:GLU63 4.6 21.4 1.0 CE2 A:TYR126 4.8 19.5 1.0 NE2 A:HIS59 4.8 19.8 1.0 CD2 A:PHE60 4.8 16.9 1.0 CE2 A:PHE60 4.8 18.6 1.0 CA A:ASP123 4.9 23.1 1.0 N A:ASP123 4.9 23.9 1.0

Iron binding site 2 out of 2 in the Deoxy-Dcrh-Hr


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Deoxy-Dcrh-Hr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe137 b:22.1 occ:1.00 FE2 A:FEO137 0.0 22.1 1.0 O A:FEO137 1.9 17.9 1.0 OD2 A:ASP123 2.1 15.4 1.0 NE2 A:HIS23 2.1 20.9 1.0 NE2 A:HIS59 2.2 19.8 1.0 OE2 A:GLU63 2.2 20.9 1.0 CG A:ASP123 3.0 18.9 1.0 CE1 A:HIS59 3.0 18.9 1.0 CE1 A:HIS23 3.0 19.2 1.0 CD A:GLU63 3.1 22.0 1.0 CD2 A:HIS23 3.2 21.1 1.0 OD1 A:ASP123 3.3 13.8 1.0 CD2 A:HIS59 3.4 18.2 1.0 FE1 A:FEO137 3.4 21.6 1.0 OE1 A:GLU63 3.6 24.1 1.0 OH A:TYR126 4.1 19.3 1.0 ND1 A:HIS59 4.2 19.5 1.0 ND1 A:HIS23 4.2 17.9 1.0 CB A:ASP123 4.2 18.9 1.0 CG A:GLU63 4.2 21.4 1.0 CG A:HIS23 4.3 20.3 1.0 CD2 A:HIS118 4.3 21.8 1.0 CG A:HIS59 4.4 20.1 1.0 NE2 A:HIS118 4.5 25.6 1.0 CG2 A:ILE19 4.7 22.4 1.0 NE2 A:HIS82 4.8 21.1 1.0 CG1 A:ILE119 4.8 22.1 1.0

C.E.Isaza, R.Silaghi-Dumitrescu, R.B.Iyer, D.M.Kurtz, M.K.Chan. Structural Basis For O(2) Sensing By the Hemerythrin-Like Domain of A Bacterial Chemotaxis Protein: Substrate Tunnel and Fluxional N Terminus Biochemistry V. 45 9023 2006.
ISSN: ISSN 0006-2960
PubMed: 16866347
DOI: 10.1021/BI0607812