Iron in PDB 4z6s: Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution, PDB code: 4z6s 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)	47.95 / 1.42
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.568, 151.990, 96.356, 90.00, 90.00, 90.00
R / Rfree (%)	12.4 / 16

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution also contains other interesting chemical elements:

Chlorine	(Cl)	3 atoms
Calcium	(Ca)	1 atom

The binding sites of Iron atom in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution (pdb code 4z6s). 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 4-Sulfonyl Catechol at 1.42 Ang Resolution, PDB code: 4z6s:
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 4-Sulfonyl Catechol at 1.42 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 4-Sulfonyl Catechol at 1.42 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:12.4 occ:1.00 OE1 A:GLU267 2.1 11.1 1.0 O A:HOH742 2.1 17.3 1.0 O A:HOH501 2.2 15.3 1.0 NE2 A:HIS214 2.2 12.2 1.0 NE2 A:HIS155 2.2 10.3 1.0 O A:HOH518 2.3 13.4 1.0 CE1 A:HIS214 3.0 12.7 1.0 CE1 A:HIS155 3.1 9.7 1.0 CD A:GLU267 3.1 12.2 1.0 CD2 A:HIS155 3.2 9.7 1.0 CD2 A:HIS214 3.3 11.4 1.0 OE2 A:GLU267 3.5 12.7 1.0 NE2 A:GLN200 4.0 13.3 1.0 OH A:TYR257 4.1 14.3 1.0 OE1 A:GLN200 4.1 16.5 1.0 ND1 A:HIS214 4.2 12.1 1.0 ND1 A:HIS155 4.2 10.6 1.0 O A:HOH811 4.3 23.6 1.0 CG A:HIS214 4.3 11.0 1.0 CG A:HIS155 4.3 10.1 1.0 CD A:GLN200 4.4 13.1 1.0 CG A:GLU267 4.4 11.2 1.0 ND2 A:ASN157 4.5 15.9 1.0 CE1 A:TYR257 4.6 12.6 1.0 CB A:GLU267 4.6 10.2 1.0 CB A:ALA216 4.6 11.0 1.0 CB A:ASN157 4.7 12.2 1.0 CZ A:TYR257 4.8 14.2 1.0 CD1 A:TYR269 5.0 13.7 1.0 CE1 A:TYR269 5.0 12.4 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 4-Sulfonyl Catechol at 1.42 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 4-Sulfonyl Catechol at 1.42 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:10.9 occ:1.00 OE1 B:GLU267 2.0 11.2 1.0 O B:HOH749 2.2 14.0 1.0 O B:HOH537 2.2 10.4 1.0 NE2 B:HIS155 2.2 9.4 1.0 NE2 B:HIS214 2.2 9.3 1.0 O B:HOH507 2.2 13.6 1.0 CE1 B:HIS214 3.1 9.8 1.0 CE1 B:HIS155 3.1 9.2 1.0 CD B:GLU267 3.1 10.2 1.0 CD2 B:HIS155 3.2 9.0 1.0 CD2 B:HIS214 3.3 9.2 1.0 OE2 B:GLU267 3.6 10.9 1.0 OE1 B:GLN200 4.0 13.3 1.0 OH B:TYR257 4.1 12.3 1.0 NE2 B:GLN200 4.1 13.8 1.0 ND1 B:HIS214 4.2 9.4 1.0 ND1 B:HIS155 4.2 9.3 1.0 O B:HOH849 4.3 21.5 1.0 CG B:HIS155 4.3 9.4 1.0 CG B:HIS214 4.4 8.9 1.0 CG B:GLU267 4.4 9.5 1.0 ND2 B:ASN157 4.4 11.2 1.0 CD B:GLN200 4.4 12.7 1.0 CB B:GLU267 4.6 9.3 1.0 CE1 B:TYR257 4.6 11.8 1.0 CB B:ASN157 4.6 9.5 1.0 CB B:ALA216 4.7 9.4 1.0 CZ B:TYR257 4.8 11.7 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 4-Sulfonyl Catechol at 1.42 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 4-Sulfonyl Catechol at 1.42 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:12.5 occ:1.00 O7 C:4SX402 2.0 14.4 1.0 OE1 C:GLU267 2.0 12.3 1.0 O8 C:4SX402 2.1 13.9 1.0 NE2 C:HIS214 2.2 10.9 1.0 NE2 C:HIS155 2.2 10.6 1.0 O C:HOH584 2.4 14.2 1.0 C1 C:4SX402 2.8 13.8 1.0 C2 C:4SX402 2.9 15.3 1.0 CE1 C:HIS214 3.0 11.2 1.0 CD C:GLU267 3.1 11.7 1.0 CE1 C:HIS155 3.1 9.9 1.0 CD2 C:HIS214 3.2 11.4 1.0 CD2 C:HIS155 3.2 11.1 1.0 OE2 C:GLU267 3.5 13.9 1.0 OH C:TYR257 4.0 14.7 1.0 NE2 C:GLN200 4.1 14.1 1.0 ND1 C:HIS214 4.2 11.7 1.0 C6 C:4SX402 4.2 12.8 1.0 OE1 C:GLN200 4.2 13.6 1.0 C3 C:4SX402 4.2 15.0 1.0 ND1 C:HIS155 4.2 9.8 1.0 CG C:HIS214 4.3 11.2 1.0 CG C:HIS155 4.3 10.5 1.0 CG C:GLU267 4.3 10.1 1.0 CB C:GLU267 4.5 9.8 1.0 CE2 C:TYR257 4.5 12.0 1.0 CD C:GLN200 4.5 13.1 1.0 ND2 C:ASN157 4.6 15.2 1.0 CB C:ALA216 4.6 9.8 1.0 CZ C:TYR257 4.8 12.6 1.0 CB C:ASN157 4.8 12.5 1.0 CD1 C:TYR269 4.8 12.7 1.0 CE1 C:TYR269 4.9 12.7 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 4-Sulfonyl Catechol at 1.42 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 4-Sulfonyl Catechol at 1.42 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:12.3 occ:1.00 OE1 D:GLU267 2.0 12.3 1.0 O7 D:4SX403 2.1 13.8 0.8 O8 D:4SX403 2.1 10.4 0.8 NE2 D:HIS214 2.2 10.5 1.0 NE2 D:HIS155 2.2 10.8 1.0 O D:HOH546 2.3 14.3 1.0 C1 D:4SX403 2.8 13.6 0.8 C2 D:4SX403 2.9 15.3 0.8 CE1 D:HIS214 3.0 11.7 1.0 CD D:GLU267 3.1 11.8 1.0 CE1 D:HIS155 3.1 10.7 1.0 CD2 D:HIS214 3.2 11.6 1.0 CD2 D:HIS155 3.2 11.0 1.0 OE2 D:GLU267 3.5 12.4 1.0 OH D:TYR257 4.0 13.3 1.0 OE1 D:GLN200 4.1 15.6 1.0 NE2 D:GLN200 4.1 14.3 1.0 ND1 D:HIS214 4.2 11.8 1.0 C3 D:4SX403 4.2 13.4 0.8 C6 D:4SX403 4.2 13.3 0.8 ND1 D:HIS155 4.2 11.6 1.0 CG D:HIS214 4.3 10.4 1.0 CG D:HIS155 4.3 11.7 1.0 CG D:GLU267 4.4 10.9 1.0 CD D:GLN200 4.5 13.9 1.0 CE1 D:TYR257 4.5 11.1 1.0 ND2 D:ASN157 4.6 14.8 1.0 CB D:GLU267 4.6 10.5 1.0 CB D:ALA216 4.6 10.7 1.0 CB D:ASN157 4.7 12.9 1.0 CZ D:TYR257 4.7 12.8 1.0 CD1 D:TYR269 4.9 12.1 1.0 CE1 D:TYR269 4.9 13.2 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