Iron in PDB 1krh: X-Ray Structure of Benzoate Dioxygenase Reductase

All present enzymatic activity of X-Ray Structure of Benzoate Dioxygenase Reductase:
1.18.1.3;

The structure of X-Ray Structure of Benzoate Dioxygenase Reductase, PDB code: 1krh was solved by A.Karlsson, Z.M.Beharry, D.M.Eby, E.D.Coulter, E.L.Niedle, D.M.Kurtz Jr., H.Eklund, S.Ramaswamy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.00 / 1.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	94.093, 100.682, 153.541, 90.00, 90.00, 90.00
R / Rfree (%)	24.1 / 24.9

The binding sites of Iron atom in the X-Ray Structure of Benzoate Dioxygenase Reductase (pdb code 1krh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the X-Ray Structure of Benzoate Dioxygenase Reductase, PDB code: 1krh:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the X-Ray Structure of Benzoate Dioxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of Benzoate Dioxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:12.9 occ:1.00 FE1 A:FES500 0.0 12.9 1.0 S1 A:FES500 2.2 11.9 1.0 S2 A:FES500 2.2 13.0 1.0 SG A:CYS49 2.3 9.2 1.0 SG A:CYS83 2.4 9.5 1.0 FE2 A:FES500 2.7 13.7 1.0 CB A:CYS83 3.3 9.8 1.0 CB A:CYS49 3.3 10.0 1.0 N A:CYS49 4.2 10.1 1.0 N A:CYS83 4.2 9.1 1.0 N A:GLY44 4.3 8.9 1.0 CA A:CYS83 4.3 9.9 1.0 CA A:CYS49 4.4 9.6 1.0 CA A:GLY44 4.4 10.0 1.0 N A:ARG42 4.5 10.0 1.0 SG A:CYS41 4.5 9.6 1.0 CB A:LEU81 4.5 10.1 1.0 CG A:MET39 4.6 12.4 1.0 CA A:ARG42 4.6 10.5 1.0 CD2 A:LEU81 4.7 10.4 1.0 SG A:CYS46 4.7 9.2 1.0 N A:GLY47 4.9 9.5 1.0 N A:GLU43 4.9 10.6 1.0 C A:ARG42 5.0 11.0 1.0

Iron binding site 2 out of 4 in the X-Ray Structure of Benzoate Dioxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Structure of Benzoate Dioxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:13.7 occ:1.00 FE2 A:FES500 0.0 13.7 1.0 S2 A:FES500 2.2 13.0 1.0 S1 A:FES500 2.2 11.9 1.0 SG A:CYS41 2.4 9.6 1.0 SG A:CYS46 2.4 9.2 1.0 FE1 A:FES500 2.7 12.9 1.0 CB A:CYS41 3.5 9.7 1.0 N A:CYS41 3.5 8.4 1.0 CB A:CYS46 3.6 9.8 1.0 N A:CYS46 3.6 9.0 1.0 N A:ARG42 3.7 10.0 1.0 N A:GLY47 3.8 9.5 1.0 CA A:CYS41 3.9 9.6 1.0 CA A:CYS46 3.9 10.2 1.0 C A:CYS41 4.2 9.6 1.0 N A:GLU45 4.2 9.1 1.0 N A:GLY44 4.3 8.9 1.0 C A:CYS46 4.3 9.9 1.0 N A:THR48 4.3 8.8 1.0 SG A:CYS83 4.4 9.5 1.0 N A:GLU43 4.5 10.6 1.0 C A:ASP40 4.5 10.8 1.0 N A:ASP40 4.6 10.2 1.0 SG A:CYS49 4.6 9.2 1.0 CA A:ARG42 4.6 10.5 1.0 CA A:GLY44 4.6 10.0 1.0 C A:GLU45 4.7 10.2 1.0 CA A:GLY47 4.8 9.8 1.0 C A:GLY44 4.8 9.6 1.0 N A:CYS49 4.8 10.1 1.0 CA A:ASP40 4.9 10.4 1.0 CB A:ASP40 4.9 9.5 1.0 CB A:THR48 4.9 9.5 1.0

Iron binding site 3 out of 4 in the X-Ray Structure of Benzoate Dioxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Structure of Benzoate Dioxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:14.4 occ:1.00 FE1 B:FES600 0.0 14.4 1.0 S2 B:FES600 2.2 15.8 1.0 S1 B:FES600 2.2 13.9 1.0 SG B:CYS49 2.2 9.5 1.0 SG B:CYS83 2.4 9.3 1.0 FE2 B:FES600 2.7 15.6 1.0 CB B:CYS49 3.3 10.1 1.0 CB B:CYS83 3.3 9.2 1.0 N B:CYS49 4.1 10.3 1.0 N B:CYS83 4.2 9.2 1.0 N B:GLY44 4.3 10.3 1.0 CA B:CYS49 4.3 9.8 1.0 CA B:CYS83 4.4 9.8 1.0 CA B:GLY44 4.5 10.4 1.0 SG B:CYS41 4.5 9.8 1.0 CB B:LEU81 4.5 9.8 1.0 N B:ARG42 4.5 9.2 1.0 CG B:MET39 4.6 12.4 1.0 CD2 B:LEU81 4.7 10.2 1.0 CA B:ARG42 4.7 11.0 1.0 SG B:CYS46 4.7 9.3 1.0 N B:GLY47 4.9 9.7 1.0 N B:GLU43 4.9 11.2 1.0 CG B:LEU81 5.0 9.3 1.0 CD1 B:LEU81 5.0 10.6 1.0

Iron binding site 4 out of 4 in the X-Ray Structure of Benzoate Dioxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Structure of Benzoate Dioxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:15.6 occ:1.00 FE2 B:FES600 0.0 15.6 1.0 S1 B:FES600 2.2 13.9 1.0 S2 B:FES600 2.2 15.8 1.0 SG B:CYS46 2.3 9.3 1.0 SG B:CYS41 2.3 9.8 1.0 FE1 B:FES600 2.7 14.4 1.0 CB B:CYS46 3.6 9.8 1.0 CB B:CYS41 3.6 9.9 1.0 N B:CYS46 3.6 9.4 1.0 N B:CYS41 3.6 8.2 1.0 N B:ARG42 3.7 9.2 1.0 N B:GLY47 3.7 9.7 1.0 CA B:CYS46 3.9 9.9 1.0 CA B:CYS41 3.9 10.1 1.0 N B:GLU45 4.2 10.3 1.0 C B:CYS46 4.3 10.1 1.0 C B:CYS41 4.3 10.1 1.0 N B:GLY44 4.3 10.3 1.0 N B:THR48 4.3 9.1 1.0 N B:GLU43 4.5 11.2 1.0 SG B:CYS83 4.5 9.3 1.0 C B:ASP40 4.5 9.6 1.0 N B:ASP40 4.5 9.6 1.0 SG B:CYS49 4.6 9.5 1.0 CA B:ARG42 4.7 11.0 1.0 CA B:GLY47 4.7 9.7 1.0 C B:GLU45 4.7 10.7 1.0 CA B:GLY44 4.7 10.4 1.0 N B:CYS49 4.8 10.3 1.0 CB B:ASP40 4.8 9.7 1.0 CA B:ASP40 4.9 9.9 1.0 C B:GLY44 4.9 10.0 1.0 C B:GLY47 4.9 9.7 1.0 CB B:THR48 5.0 9.6 1.0

A.Karlsson, Z.M.Beharry, D.Matthew Eby, E.D.Coulter, E.L.Neidle, D.M.Kurtz Jr., H.Eklund, S.Ramaswamy. X-Ray Crystal Structure of Benzoate 1,2-Dioxygenase Reductase From Acinetobacter Sp. Strain ADP1. J.Mol.Biol. V. 318 261 2002.
ISSN: ISSN 0022-2836
PubMed: 12051836
DOI: 10.1016/S0022-2836(02)00039-6