Iron in PDB 5bwh: Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution, PDB code: 5bwh 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)	29.66 / 1.46
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.414, 151.027, 96.468, 90.00, 90.00, 90.00
R / Rfree (%)	12.2 / 16.1

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution also contains other interesting chemical elements:

Chlorine	(Cl)	2 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 in Complex with Hpca at 1.46 Ang Resolution (pdb code 5bwh). 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 in Complex with Hpca at 1.46 Ang Resolution, PDB code: 5bwh:
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 in Complex with Hpca at 1.46 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 in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:18.1 occ:1.00 OE1 A:GLU267 2.1 14.6 1.0 O A:HOH760 2.1 22.0 1.0 O A:HOH504 2.2 19.8 1.0 NE2 A:HIS155 2.2 15.6 1.0 NE2 A:HIS214 2.2 15.2 1.0 O A:HOH707 2.3 17.2 1.0 CE1 A:HIS214 3.1 16.5 1.0 CE1 A:HIS155 3.1 15.4 1.0 CD A:GLU267 3.1 15.9 1.0 CD2 A:HIS155 3.3 17.1 1.0 CD2 A:HIS214 3.3 15.3 1.0 OE2 A:GLU267 3.5 16.0 1.0 OH A:TYR257 4.1 15.7 1.0 ND1 A:HIS214 4.2 16.4 1.0 O A:HOH788 4.2 32.1 1.0 ND1 A:HIS155 4.3 15.1 1.0 CG A:HIS155 4.4 16.1 1.0 CG A:HIS214 4.4 14.9 1.0 O A:HOH715 4.4 25.6 1.0 CG A:GLU267 4.4 15.4 1.0 ND2 A:ASN157 4.4 19.3 1.0 O A:HOH795 4.5 32.6 1.0 CB A:GLU267 4.6 14.1 1.0 CB A:ALA216 4.6 14.9 1.0 CB A:ASN157 4.7 16.8 1.0 CE1 A:TYR257 4.7 14.2 1.0 NE1 A:TRP192 4.8 19.5 1.0 CZ A:TYR257 4.9 15.6 1.0

Iron binding site 2 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:16.4 occ:1.00 OE1 B:GLU267 2.1 14.2 1.0 O B:HOH503 2.1 18.8 1.0 NE2 B:HIS214 2.2 13.3 1.0 O B:HOH759 2.2 22.2 1.0 NE2 B:HIS155 2.2 13.4 1.0 O B:HOH772 2.2 14.0 1.0 CE1 B:HIS214 3.0 14.7 1.0 CE1 B:HIS155 3.1 13.7 1.0 CD B:GLU267 3.1 14.2 1.0 CD2 B:HIS155 3.3 13.9 1.0 CD2 B:HIS214 3.3 13.8 1.0 OE2 B:GLU267 3.6 16.4 1.0 OH B:TYR257 4.1 15.6 1.0 ND1 B:HIS214 4.2 14.2 1.0 ND1 B:HIS155 4.3 13.9 1.0 O B:HOH813 4.3 30.3 1.0 CG B:HIS214 4.3 13.8 1.0 CG B:HIS155 4.4 15.1 1.0 ND2 B:ASN157 4.4 15.9 1.0 CG B:GLU267 4.4 12.6 1.0 O B:HOH811 4.4 31.7 1.0 O B:HOH738 4.4 26.4 1.0 CB B:GLU267 4.6 11.5 1.0 CB B:ALA216 4.6 13.2 1.0 CB B:ASN157 4.6 13.7 1.0 CE1 B:TYR257 4.7 12.8 1.0 NE1 B:TRP192 4.7 19.5 1.0 CZ B:TYR257 4.9 12.8 1.0

Iron binding site 3 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:17.2 occ:1.00 OE1 C:GLU267 2.0 14.4 1.0 O3 C:DHY403 2.1 17.4 1.0 O4 C:DHY403 2.1 18.6 1.0 NE2 C:HIS214 2.2 12.9 1.0 NE2 C:HIS155 2.3 14.7 1.0 O C:HOH699 2.5 17.1 1.0 C3 C:DHY403 2.8 17.2 1.0 C4 C:DHY403 2.9 18.1 1.0 CE1 C:HIS214 3.1 14.3 1.0 CD C:GLU267 3.1 14.6 1.0 CE1 C:HIS155 3.1 14.4 1.0 CD2 C:HIS214 3.3 14.5 1.0 CD2 C:HIS155 3.3 13.6 1.0 OE2 C:GLU267 3.5 17.4 1.0 OH C:TYR257 4.2 15.0 1.0 C2 C:DHY403 4.2 18.2 1.0 C5 C:DHY403 4.2 18.5 1.0 ND1 C:HIS214 4.2 13.8 1.0 ND1 C:HIS155 4.3 14.6 1.0 CG C:GLU267 4.4 13.1 1.0 CG C:HIS214 4.4 13.5 1.0 CG C:HIS155 4.4 14.2 1.0 O C:HOH621 4.4 23.7 1.0 CB C:GLU267 4.5 13.2 1.0 CB C:ALA216 4.5 12.6 1.0 ND2 C:ASN157 4.6 17.1 1.0 CE1 C:TYR257 4.6 13.7 1.0 CB C:ASN157 4.7 15.2 1.0 CZ C:TYR257 4.9 12.1 1.0 CD1 C:TYR269 4.9 17.3 1.0 CE1 C:TYR269 4.9 15.4 1.0 NE1 C:TRP192 4.9 19.4 1.0

Iron binding site 4 out of 4 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:15.8 occ:1.00 OE1 D:GLU267 2.0 13.7 1.0 O3 D:DHY403 2.0 15.8 1.0 O4 D:DHY403 2.1 16.7 1.0 NE2 D:HIS155 2.2 13.9 1.0 NE2 D:HIS214 2.2 12.4 1.0 O D:HOH707 2.4 17.2 1.0 C3 D:DHY403 2.9 15.7 1.0 C4 D:DHY403 2.9 16.7 1.0 CE1 D:HIS214 3.1 13.2 1.0 CD D:GLU267 3.1 15.2 1.0 CE1 D:HIS155 3.1 14.0 1.0 CD2 D:HIS214 3.3 13.2 1.0 CD2 D:HIS155 3.3 16.1 1.0 OE2 D:GLU267 3.5 14.5 1.0 OH D:TYR257 4.1 14.1 1.0 ND1 D:HIS214 4.2 13.1 1.0 C2 D:DHY403 4.2 16.6 1.0 ND1 D:HIS155 4.2 15.4 1.0 C5 D:DHY403 4.3 15.0 1.0 CG D:GLU267 4.4 13.3 1.0 CG D:HIS214 4.4 12.9 1.0 CG D:HIS155 4.4 13.8 1.0 O D:HOH669 4.4 20.4 1.0 ND2 D:ASN157 4.5 17.7 1.0 CB D:GLU267 4.6 12.6 1.0 CB D:ALA216 4.6 13.2 1.0 CE1 D:TYR257 4.6 11.3 1.0 CB D:ASN157 4.7 13.4 1.0 CZ D:TYR257 4.8 12.3 1.0 NE1 D:TRP192 4.9 19.3 1.0 CE1 D:TYR269 4.9 15.1 1.0 CD1 D:TYR269 5.0 14.2 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