Iron in PDB 4z6p: Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution, PDB code: 4z6p 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)	40.54 / 1.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.794, 151.235, 96.388, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 17.7

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Iron atom in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution (pdb code 4z6p). 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution, PDB code: 4z6p:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:19.8 occ:1.00 OE1 A:GLU267 2.1 18.5 1.0 O A:HOH694 2.2 20.4 1.0 O A:HOH516 2.2 16.2 1.0 NE2 A:HIS155 2.2 17.9 1.0 O A:HOH504 2.2 19.1 1.0 NE2 A:HIS214 2.3 18.9 1.0 CE1 A:HIS155 3.1 17.8 1.0 CE1 A:HIS214 3.1 18.4 1.0 CD A:GLU267 3.2 19.1 1.0 CD2 A:HIS155 3.3 18.4 1.0 CD2 A:HIS214 3.3 18.6 1.0 OE2 A:GLU267 3.6 18.9 1.0 NE2 A:GLN200 4.0 18.2 1.0 OE1 A:GLN200 4.1 20.7 1.0 OH A:TYR257 4.1 17.1 1.0 ND1 A:HIS214 4.2 18.9 1.0 ND1 A:HIS155 4.2 19.1 1.0 O A:HOH742 4.3 30.1 1.0 ND2 A:ASN157 4.4 19.6 1.0 CG A:HIS155 4.4 17.9 1.0 CG A:HIS214 4.4 18.7 1.0 CD A:GLN200 4.4 18.1 1.0 CG A:GLU267 4.4 17.5 1.0 CB A:GLU267 4.6 17.2 1.0 CE1 A:TYR257 4.6 16.7 1.0 CB A:ASN157 4.6 19.1 1.0 CB A:ALA216 4.7 18.1 1.0 CZ A:TYR257 4.9 16.8 1.0 CG A:ASN157 5.0 19.1 1.0

Iron binding site 2 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:18.5 occ:1.00 OE1 B:GLU267 2.1 15.8 1.0 O B:HOH716 2.1 20.5 1.0 O B:HOH546 2.1 13.7 1.0 O B:HOH501 2.2 17.6 1.0 NE2 B:HIS155 2.3 14.8 1.0 NE2 B:HIS214 2.3 16.4 1.0 CD B:GLU267 3.1 17.1 1.0 CE1 B:HIS214 3.1 16.0 1.0 CE1 B:HIS155 3.1 14.8 1.0 CD2 B:HIS155 3.3 15.6 1.0 CD2 B:HIS214 3.3 16.0 1.0 OE2 B:GLU267 3.5 17.2 1.0 NE2 B:GLN200 4.0 16.7 1.0 OE1 B:GLN200 4.1 19.2 1.0 OH B:TYR257 4.1 16.6 1.0 O B:HOH751 4.2 27.6 1.0 ND1 B:HIS214 4.3 17.1 1.0 ND1 B:HIS155 4.3 16.2 1.0 ND2 B:ASN157 4.4 17.1 1.0 CD B:GLN200 4.4 17.5 1.0 CG B:HIS155 4.4 15.4 1.0 CG B:GLU267 4.4 15.9 1.0 CG B:HIS214 4.4 16.0 1.0 CB B:GLU267 4.6 15.9 1.0 CB B:ASN157 4.6 17.8 1.0 CE1 B:TYR257 4.7 16.0 1.0 CB B:ALA216 4.8 16.0 1.0 CZ B:TYR257 4.9 16.5 1.0

Iron binding site 3 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:18.8 occ:1.00 OE1 C:GLU267 2.0 17.2 1.0 O4 C:DHY403 2.1 19.5 1.0 O3 C:DHY403 2.1 17.1 1.0 NE2 C:HIS155 2.3 14.6 1.0 NE2 C:HIS214 2.3 15.6 1.0 O C:HOH595 2.4 16.6 1.0 C4 C:DHY403 2.8 23.1 1.0 C3 C:DHY403 2.8 23.7 1.0 CD C:GLU267 3.1 16.1 1.0 CE1 C:HIS214 3.1 15.7 1.0 CE1 C:HIS155 3.2 15.4 1.0 CD2 C:HIS155 3.3 15.9 1.0 CD2 C:HIS214 3.3 15.9 1.0 OE2 C:GLU267 3.5 18.4 1.0 NE2 C:GLN200 4.1 16.2 1.0 OE1 C:GLN200 4.1 20.8 1.0 OH C:TYR257 4.1 17.8 1.0 C5 C:DHY403 4.2 19.5 1.0 C2 C:DHY403 4.2 23.0 1.0 ND1 C:HIS155 4.3 15.1 1.0 ND1 C:HIS214 4.3 15.5 1.0 CG C:GLU267 4.4 15.6 1.0 CG C:HIS155 4.4 15.9 1.0 CG C:HIS214 4.4 15.4 1.0 CD C:GLN200 4.5 16.9 1.0 ND2 C:ASN157 4.5 18.4 1.0 CB C:GLU267 4.5 15.1 1.0 CE1 C:TYR257 4.6 16.2 1.0 CB C:ALA216 4.7 16.0 1.0 CB C:ASN157 4.7 17.7 1.0 CZ C:TYR257 4.9 16.2 1.0 CD2 C:TYR269 4.9 15.2 1.0

Iron binding site 4 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.75 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:18.4 occ:1.00 OE1 D:GLU267 2.0 16.1 1.0 O D:HOH700 2.1 18.5 1.0 O D:HOH631 2.1 15.4 1.0 O D:HOH508 2.2 20.4 1.0 NE2 D:HIS214 2.2 15.3 1.0 NE2 D:HIS155 2.3 16.3 1.0 CE1 D:HIS214 3.0 15.5 1.0 CD D:GLU267 3.1 16.8 1.0 CE1 D:HIS155 3.2 16.1 1.0 CD2 D:HIS214 3.3 15.8 1.0 CD2 D:HIS155 3.3 16.2 1.0 OE2 D:GLU267 3.5 16.4 1.0 NE2 D:GLN200 4.0 16.8 1.0 OE1 D:GLN200 4.1 19.2 1.0 OH D:TYR257 4.1 16.3 1.0 ND1 D:HIS214 4.2 16.1 1.0 O D:HOH762 4.2 26.1 1.0 ND1 D:HIS155 4.3 17.3 1.0 CG D:HIS214 4.3 15.5 1.0 ND2 D:ASN157 4.3 18.4 1.0 CG D:HIS155 4.4 16.5 1.0 CG D:GLU267 4.4 16.4 1.0 CD D:GLN200 4.4 18.1 1.0 CB D:ASN157 4.6 16.9 1.0 CE1 D:TYR257 4.6 15.8 1.0 CB D:GLU267 4.7 15.2 1.0 CB D:ALA216 4.7 14.9 1.0 CZ D:TYR257 4.8 15.7 1.0 CG D:ASN157 5.0 18.1 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