Iron in PDB 2avk: Met-Azido-Dcrh-Hr

The structure of Met-Azido-Dcrh-Hr, PDB code: 2avk 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)	19.87 / 1.53
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.450, 49.580, 69.000, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 23.5

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

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Met-Azido-Dcrh-Hr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:6.9 occ:1.00 FE1 A:FEA201 0.0 6.9 1.0 O A:FEA201 1.9 8.9 1.0 OE1 A:GLU63 2.2 7.4 1.0 NE2 A:HIS118 2.2 6.9 1.0 OD1 A:ASP123 2.2 8.5 1.0 NE2 A:HIS82 2.2 7.2 1.0 NE2 A:HIS78 2.2 8.1 1.0 CD A:GLU63 3.1 9.2 1.0 CE1 A:HIS82 3.1 7.4 1.0 CD2 A:HIS118 3.1 5.3 1.0 CE1 A:HIS78 3.2 7.5 1.0 CG A:ASP123 3.2 6.8 1.0 CE1 A:HIS118 3.2 7.3 1.0 FE2 A:FEA201 3.2 6.7 1.0 OE2 A:GLU63 3.3 6.8 1.0 CD2 A:HIS78 3.3 8.0 1.0 CD2 A:HIS82 3.3 7.1 1.0 OD2 A:ASP123 3.4 6.8 1.0 CG A:HIS118 4.3 6.2 1.0 ND1 A:HIS82 4.3 8.0 1.0 ND1 A:HIS118 4.3 7.2 1.0 ND1 A:HIS78 4.3 9.4 1.0 CG A:GLU63 4.4 9.6 1.0 CG A:HIS82 4.4 8.1 1.0 CG A:HIS78 4.4 7.7 1.0 NA A:FEA201 4.5 8.9 1.0 CB A:ASP123 4.6 8.2 1.0 NE2 A:HIS59 4.6 6.7 1.0 CD2 A:PHE60 4.7 8.0 1.0 CE2 A:PHE60 4.7 10.3 1.0 CE2 A:TYR126 4.7 8.0 1.0 NB A:FEA201 4.8 12.5 1.0 CB A:GLU63 4.8 8.0 1.0 CA A:ASP123 4.9 9.9 1.0

Iron binding site 2 out of 2 in the Met-Azido-Dcrh-Hr


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Met-Azido-Dcrh-Hr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:6.7 occ:1.00 FE2 A:FEA201 0.0 6.7 1.0 O A:FEA201 1.8 8.9 1.0 NA A:FEA201 2.1 8.9 1.0 OD2 A:ASP123 2.1 6.8 1.0 NE2 A:HIS59 2.2 6.7 1.0 OE2 A:GLU63 2.2 6.8 1.0 NE2 A:HIS23 2.2 6.2 1.0 NB A:FEA201 3.0 12.5 1.0 CG A:ASP123 3.0 6.8 1.0 CD A:GLU63 3.1 9.2 1.0 CE1 A:HIS59 3.1 7.5 1.0 CD2 A:HIS59 3.2 7.9 1.0 CD2 A:HIS23 3.2 7.7 1.0 CE1 A:HIS23 3.2 7.3 1.0 FE1 A:FEA201 3.2 6.9 1.0 OD1 A:ASP123 3.4 8.5 1.0 OE1 A:GLU63 3.5 7.4 1.0 CD2 A:HIS118 4.0 5.3 1.0 NC A:FEA201 4.0 14.9 1.0 NE2 A:HIS118 4.2 6.9 1.0 CG A:GLU63 4.3 9.6 1.0 CB A:ASP123 4.3 8.2 1.0 ND1 A:HIS59 4.3 7.3 1.0 OH A:TYR126 4.3 9.5 1.0 ND1 A:HIS23 4.3 8.0 1.0 CG A:HIS59 4.3 7.5 1.0 CG A:HIS23 4.3 6.0 1.0 CG1 A:ILE119 4.7 9.6 1.0 NE2 A:HIS82 4.8 7.2 1.0 CE2 A:PHE60 5.0 10.3 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