Iron in PDB 5bwg: Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution, PDB code: 5bwg was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.73 / 1.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.748, 150.627, 96.269, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 17.9

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Calcium	(Ca)	1 atom

The binding sites of Iron atom in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution (pdb code 5bwg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution, PDB code: 5bwg:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:26.3 occ:1.00 OE1 A:GLU267 2.1 23.3 1.0 O A:HOH707 2.2 23.6 1.0 O A:HOH713 2.2 22.3 1.0 NE2 A:HIS155 2.2 24.0 1.0 NE2 A:HIS214 2.2 23.8 1.0 O A:HOH504 2.3 29.6 1.0 CE1 A:HIS214 3.0 23.1 1.0 CE1 A:HIS155 3.1 26.1 1.0 CD A:GLU267 3.2 23.8 1.0 CD2 A:HIS155 3.2 25.7 1.0 CD2 A:HIS214 3.3 23.6 1.0 OE2 A:GLU267 3.6 23.4 1.0 ND1 A:HIS214 4.2 23.5 1.0 OH A:TYR257 4.2 23.9 1.0 ND1 A:HIS155 4.3 25.3 1.0 O A:HOH779 4.3 43.9 1.0 CG A:HIS155 4.3 26.3 1.0 ND2 A:ASN157 4.3 24.8 1.0 CG A:HIS214 4.4 23.9 1.0 O A:HOH682 4.4 24.1 0.6 CG A:GLU267 4.5 21.6 1.0 CB A:ASN157 4.6 24.1 1.0 NE1 A:TRP192 4.6 28.4 1.0 CB A:GLU267 4.7 20.3 1.0 CB A:ALA216 4.7 22.4 1.0 CE1 A:TYR257 4.7 20.9 1.0 CZ A:TYR257 5.0 21.2 1.0 CG A:ASN157 5.0 25.1 1.0

Iron binding site 2 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:25.0 occ:1.00 OE1 B:GLU267 2.1 20.4 1.0 O B:HOH741 2.1 21.7 1.0 NE2 B:HIS155 2.2 19.3 1.0 O B:HOH508 2.2 23.9 1.0 NE2 B:HIS214 2.3 19.1 1.0 O B:HOH737 2.3 28.4 1.0 CE1 B:HIS214 3.1 17.8 1.0 CE1 B:HIS155 3.1 20.8 1.0 CD B:GLU267 3.2 20.8 1.0 CD2 B:HIS155 3.2 22.7 1.0 CD2 B:HIS214 3.4 18.4 1.0 OE2 B:GLU267 3.6 23.0 1.0 OH B:TYR257 4.2 21.7 1.0 ND1 B:HIS214 4.2 20.5 1.0 ND1 B:HIS155 4.3 19.6 1.0 O B:HOH797 4.3 45.5 1.0 ND2 B:ASN157 4.3 22.4 1.0 CG B:HIS155 4.3 22.2 1.0 CG B:HIS214 4.4 17.8 1.0 O B:HOH731 4.4 24.5 0.6 CG B:GLU267 4.5 18.3 1.0 CB B:ASN157 4.6 21.9 1.0 CB B:GLU267 4.6 18.1 1.0 NE1 B:TRP192 4.7 30.9 1.0 CE1 B:TYR257 4.7 19.0 1.0 CB B:ALA216 4.7 19.4 1.0 CZ B:TYR257 4.9 21.6 1.0 CG B:ASN157 5.0 22.8 1.0

Iron binding site 3 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:25.3 occ:1.00 OE1 C:GLU267 2.1 21.3 1.0 O C:HOH684 2.1 20.5 1.0 O C:HOH527 2.2 24.8 1.0 NE2 C:HIS214 2.3 18.4 1.0 O C:HOH709 2.3 25.3 1.0 NE2 C:HIS155 2.3 20.7 1.0 CE1 C:HIS214 3.1 21.6 1.0 CD C:GLU267 3.2 23.3 1.0 CE1 C:HIS155 3.2 23.5 1.0 CD2 C:HIS214 3.3 18.5 1.0 CD2 C:HIS155 3.4 22.7 1.0 OE2 C:GLU267 3.6 24.0 1.0 OH C:TYR257 4.2 22.6 1.0 ND1 C:HIS214 4.2 19.9 1.0 ND2 C:ASN157 4.3 22.1 1.0 O C:HOH768 4.3 39.1 1.0 ND1 C:HIS155 4.4 21.9 1.0 CG C:HIS214 4.4 18.5 1.0 CG C:GLU267 4.4 19.3 1.0 CG C:HIS155 4.5 22.5 1.0 CB C:ASN157 4.6 20.6 1.0 O C:HOH617 4.6 26.7 0.6 CB C:GLU267 4.6 18.4 1.0 NE1 C:TRP192 4.7 30.8 1.0 CB C:ALA216 4.7 19.6 1.0 CE1 C:TYR257 4.7 22.1 1.0 CZ C:TYR257 4.9 21.4 1.0 CG C:ASN157 4.9 21.4 1.0

Iron binding site 4 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:24.3 occ:1.00 O D:HOH700 2.1 22.8 1.0 OE1 D:GLU267 2.1 20.2 1.0 O D:HOH506 2.2 27.7 1.0 NE2 D:HIS214 2.2 16.8 1.0 NE2 D:HIS155 2.3 22.6 1.0 O D:HOH733 2.3 26.3 1.0 CE1 D:HIS214 3.1 19.4 1.0 CD D:GLU267 3.1 21.2 1.0 CE1 D:HIS155 3.2 22.2 1.0 CD2 D:HIS155 3.3 21.0 1.0 CD2 D:HIS214 3.3 19.1 1.0 OE2 D:GLU267 3.5 21.7 1.0 OH D:TYR257 4.2 20.9 1.0 ND1 D:HIS214 4.2 19.8 1.0 ND1 D:HIS155 4.3 25.1 1.0 ND2 D:ASN157 4.3 22.2 1.0 O D:HOH785 4.4 39.9 1.0 CG D:HIS214 4.4 18.2 1.0 CG D:HIS155 4.4 21.9 1.0 CG D:GLU267 4.4 18.8 1.0 CB D:ASN157 4.6 19.4 1.0 O D:HOH563 4.6 22.6 0.6 CB D:ALA216 4.6 18.4 1.0 CB D:GLU267 4.6 16.7 1.0 NE1 D:TRP192 4.7 28.1 1.0 CE1 D:TYR257 4.7 18.5 1.0 CZ D:TYR257 4.9 19.8 1.0 CG D:ASN157 5.0 21.4 1.0

K.K.Meier, M.S.Rogers, E.G.Kovaleva, M.M.Mbughuni, E.L.Bominaar, J.D.Lipscomb, E.Munck. A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization By Mossbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorg.Chem. V. 54 10269 2015.
ISSN: ISSN 0020-1669
PubMed: 26485328
DOI: 10.1021/ACS.INORGCHEM.5B01576