Iron in PDB 4z6q: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution, PDB code: 4z6q 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)	45.69 / 1.57
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.507, 150.077, 95.936, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 16.5

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution (pdb code 4z6q). 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution, PDB code: 4z6q:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:17.0 occ:1.00 OE1 A:GLU267 2.1 14.9 1.0 O A:HOH779 2.1 17.6 1.0 O A:HOH506 2.2 19.9 1.0 NE2 A:HIS214 2.2 13.9 1.0 NE2 A:HIS155 2.2 15.8 1.0 O A:HOH741 2.3 15.2 1.0 CE1 A:HIS214 3.0 14.4 1.0 CE1 A:HIS155 3.1 15.8 1.0 CD A:GLU267 3.1 14.8 1.0 CD2 A:HIS155 3.2 15.7 1.0 CD2 A:HIS214 3.3 14.4 1.0 OE2 A:GLU267 3.6 14.9 1.0 OH A:TYR257 4.1 16.2 1.0 ND1 A:HIS214 4.2 14.0 1.0 ND1 A:HIS155 4.2 15.2 1.0 O A:HOH823 4.3 31.1 1.0 O A:HOH524 4.3 26.4 1.0 CG A:HIS155 4.4 15.6 1.0 CG A:HIS214 4.4 14.6 1.0 ND2 A:ASN157 4.4 15.5 1.0 CG A:GLU267 4.4 13.4 1.0 CB A:ASN157 4.6 14.5 1.0 CB A:GLU267 4.7 12.9 1.0 CB A:ALA216 4.7 13.4 1.0 CE1 A:TYR257 4.7 14.1 1.0 NE1 A:TRP192 4.8 16.9 1.0 CZ A:TYR257 4.9 13.7 1.0 CE1 A:TYR269 5.0 16.9 1.0 CD1 A:TYR269 5.0 16.1 1.0

Iron binding site 2 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:15.3 occ:1.00 OE1 B:GLU267 2.0 15.7 1.0 O B:HOH508 2.1 19.4 1.0 NE2 B:HIS155 2.2 11.7 1.0 O B:HOH740 2.2 13.7 1.0 O B:HOH766 2.2 20.8 1.0 NE2 B:HIS214 2.2 12.8 1.0 CE1 B:HIS214 3.0 12.7 1.0 CD B:GLU267 3.1 14.6 1.0 CE1 B:HIS155 3.1 13.1 1.0 CD2 B:HIS155 3.2 14.0 1.0 CD2 B:HIS214 3.3 12.4 1.0 OE2 B:GLU267 3.6 17.1 1.0 OH B:TYR257 4.1 16.0 1.0 O B:HOH824 4.2 30.7 1.0 ND1 B:HIS214 4.2 13.0 1.0 O B:HOH526 4.2 29.0 1.0 O B:HOH823 4.2 39.8 1.0 ND1 B:HIS155 4.2 13.0 1.0 CG B:HIS155 4.3 13.2 1.0 ND2 B:ASN157 4.3 14.1 1.0 CG B:HIS214 4.4 12.3 1.0 CG B:GLU267 4.4 12.7 1.0 CB B:GLU267 4.6 12.6 1.0 CE1 B:TYR257 4.6 13.7 1.0 CB B:ASN157 4.6 12.9 1.0 CB B:ALA216 4.7 12.6 1.0 NE1 B:TRP192 4.8 19.3 1.0 CZ B:TYR257 4.8 13.5 1.0

Iron binding site 3 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:15.4 occ:1.00 OE1 C:GLU267 2.0 13.3 1.0 O3 C:DHY403 2.1 14.2 1.0 O4 C:DHY403 2.1 17.1 1.0 NE2 C:HIS155 2.2 12.8 1.0 NE2 C:HIS214 2.2 11.8 1.0 O C:HOH713 2.6 12.5 1.0 C3 C:DHY403 2.8 15.2 1.0 C4 C:DHY403 2.8 15.8 1.0 CD C:GLU267 3.0 13.2 1.0 CE1 C:HIS155 3.1 13.5 1.0 CE1 C:HIS214 3.1 12.7 1.0 CD2 C:HIS155 3.3 12.9 1.0 CD2 C:HIS214 3.3 12.2 1.0 OE2 C:GLU267 3.5 14.2 1.0 OH C:TYR257 4.1 12.9 1.0 C2 C:DHY403 4.2 14.1 1.0 C5 C:DHY403 4.2 14.3 1.0 ND1 C:HIS214 4.2 12.8 1.0 ND1 C:HIS155 4.2 12.3 1.0 CG C:GLU267 4.3 12.4 1.0 O C:HOH504 4.3 31.5 1.0 CG C:HIS155 4.4 12.8 1.0 CG C:HIS214 4.4 11.6 1.0 CB C:GLU267 4.5 12.2 1.0 CB C:ALA216 4.5 11.5 1.0 CE1 C:TYR257 4.6 12.3 1.0 ND2 C:ASN157 4.6 14.2 1.0 CB C:ASN157 4.7 13.2 1.0 CZ C:TYR257 4.8 12.4 1.0 CD2 C:TYR269 4.8 15.9 1.0 CE2 C:TYR269 4.8 15.5 1.0 ND2 C:ASN200 4.9 18.4 1.0 NE2 C:HIS248 5.0 13.5 1.0

Iron binding site 4 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:16.0 occ:1.00 OE1 D:GLU267 2.0 12.8 1.0 O3 D:DHY403 2.1 15.9 1.0 O4 D:DHY403 2.2 18.2 1.0 NE2 D:HIS214 2.2 11.2 1.0 NE2 D:HIS155 2.2 12.6 1.0 O D:HOH703 2.5 12.4 1.0 C3 D:DHY403 2.8 17.6 1.0 C4 D:DHY403 2.9 20.5 1.0 CD D:GLU267 3.0 14.2 1.0 CE1 D:HIS214 3.1 12.4 1.0 CE1 D:HIS155 3.1 12.2 1.0 CD2 D:HIS214 3.3 11.9 1.0 CD2 D:HIS155 3.3 12.9 1.0 OE2 D:GLU267 3.5 15.3 1.0 OH D:TYR257 4.1 13.9 1.0 C2 D:DHY403 4.2 17.5 1.0 ND1 D:HIS214 4.2 12.2 1.0 C5 D:DHY403 4.2 18.2 1.0 ND1 D:HIS155 4.3 13.6 1.0 CG D:GLU267 4.3 12.7 1.0 CG D:HIS214 4.3 12.1 1.0 CG D:HIS155 4.4 12.7 1.0 O D:HOH506 4.4 29.6 1.0 ND2 D:ASN157 4.5 14.8 1.0 CB D:ALA216 4.6 11.6 1.0 CB D:GLU267 4.6 12.4 1.0 CE1 D:TYR257 4.6 12.4 1.0 CB D:ASN157 4.7 12.9 1.0 CZ D:TYR257 4.8 12.8 1.0 CD1 D:TYR269 4.9 13.1 1.0 NE1 D:TRP192 4.9 15.2 1.0 CE1 D:TYR269 5.0 13.8 1.0 ND2 D:ASN200 5.0 19.8 1.0

E.G.Kovaleva, M.S.Rogers, J.D.Lipscomb. Structural Basis For Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200. Biochemistry V. 54 5329 2015.
ISSN: ISSN 0006-2960
PubMed: 26267790
DOI: 10.1021/ACS.BIOCHEM.5B00709