Iron in PDB 4z6n: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution, PDB code: 4z6n 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)	45.76 / 1.52
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.179, 150.663, 96.067, 90.00, 90.00, 90.00
R / Rfree (%)	11.8 / 16.7

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution (pdb code 4z6n). 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 at 1.52 Ang Resolution, PDB code: 4z6n:
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 at 1.52 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 at 1.52 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 16.4 1.0 O A:HOH726 2.2 20.2 1.0 O A:HOH744 2.2 19.2 1.0 NE2 A:HIS155 2.2 17.9 1.0 NE2 A:HIS214 2.2 17.2 1.0 O A:HOH506 2.3 21.1 1.0 CE1 A:HIS214 3.1 16.7 1.0 CE1 A:HIS155 3.1 19.6 1.0 CD A:GLU267 3.2 17.8 1.0 CD2 A:HIS155 3.2 16.4 1.0 CD2 A:HIS214 3.2 15.9 1.0 OE2 A:GLU267 3.6 17.6 1.0 OH A:TYR257 4.2 17.2 1.0 ND1 A:HIS214 4.2 18.5 1.0 ND1 A:HIS155 4.2 18.3 1.0 O A:HOH813 4.3 36.4 1.0 O A:HOH534 4.3 31.4 1.0 CG A:HIS155 4.3 19.8 1.0 CG A:HIS214 4.3 17.3 1.0 ND2 A:ASN157 4.4 19.0 1.0 CG A:GLU267 4.4 15.7 1.0 CB A:ALA216 4.6 18.3 1.0 CB A:GLU267 4.6 13.8 1.0 CB A:ASN157 4.6 18.1 1.0 CE1 A:TYR257 4.7 16.7 1.0 NE1 A:TRP192 4.8 22.9 1.0 ND2 A:ASN200 4.8 28.2 1.0 CZ A:TYR257 4.9 17.2 1.0 CE1 A:TYR269 5.0 16.7 1.0 CD1 A:TYR269 5.0 19.3 1.0

Iron binding site 2 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 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 at 1.52 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:16.5 occ:1.00 OE1 B:GLU267 2.0 16.5 1.0 O B:HOH518 2.1 19.7 1.0 O B:HOH785 2.2 18.5 1.0 O B:HOH770 2.2 20.1 1.0 NE2 B:HIS155 2.2 14.3 1.0 NE2 B:HIS214 2.2 14.9 1.0 CD B:GLU267 3.1 14.6 1.0 CE1 B:HIS214 3.1 16.9 1.0 CE1 B:HIS155 3.2 14.2 1.0 CD2 B:HIS155 3.2 14.8 1.0 CD2 B:HIS214 3.3 14.7 1.0 OE2 B:GLU267 3.5 18.3 1.0 OH B:TYR257 4.2 16.7 1.0 O B:HOH826 4.2 38.0 1.0 ND1 B:HIS214 4.2 15.7 1.0 ND1 B:HIS155 4.3 14.2 1.0 O B:HOH543 4.3 35.6 1.0 CG B:HIS155 4.3 14.4 1.0 ND2 B:ASN157 4.3 16.7 1.0 CG B:HIS214 4.4 17.3 1.0 CG B:GLU267 4.4 14.7 1.0 CB B:GLU267 4.6 14.0 1.0 CB B:ALA216 4.6 15.5 1.0 CB B:ASN157 4.6 16.8 1.0 CE1 B:TYR257 4.7 15.1 1.0 NE1 B:TRP192 4.8 22.5 1.0 ND2 B:ASN200 4.8 27.8 1.0 CZ B:TYR257 4.9 15.3 1.0

Iron binding site 3 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 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 at 1.52 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:15.7 occ:1.00 OE1 C:GLU267 2.0 14.6 1.0 O C:HOH708 2.2 18.3 1.0 NE2 C:HIS214 2.2 13.1 1.0 O C:HOH724 2.2 18.0 1.0 NE2 C:HIS155 2.2 15.6 1.0 O C:HOH507 2.3 20.2 1.0 CE1 C:HIS214 3.0 15.3 1.0 CD C:GLU267 3.1 14.8 1.0 CE1 C:HIS155 3.1 14.1 1.0 CD2 C:HIS214 3.3 14.3 1.0 CD2 C:HIS155 3.3 13.1 1.0 OE2 C:GLU267 3.5 17.0 1.0 O C:HOH825 4.2 25.3 0.5 OH C:TYR257 4.2 16.5 1.0 ND1 C:HIS214 4.2 13.3 1.0 ND1 C:HIS155 4.3 13.2 1.0 O C:HOH808 4.3 31.6 1.0 ND2 C:ASN157 4.3 15.5 1.0 CG C:HIS214 4.4 13.6 1.0 CG C:GLU267 4.4 13.6 1.0 CG C:HIS155 4.4 13.0 1.0 O C:HOH531 4.4 30.6 1.0 CB C:ASN157 4.6 14.8 1.0 CB C:GLU267 4.6 12.6 1.0 CE1 C:TYR257 4.6 14.7 1.0 CB C:ALA216 4.7 14.4 1.0 ND2 C:ASN200 4.7 25.9 1.0 NE1 C:TRP192 4.8 23.8 1.0 CZ C:TYR257 4.9 14.4 1.0 CG C:ASN157 4.9 13.2 1.0

Iron binding site 4 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 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 at 1.52 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:15.4 occ:1.00 OE1 D:GLU267 2.1 14.2 1.0 O D:HOH512 2.1 18.8 1.0 O D:HOH758 2.2 17.6 1.0 NE2 D:HIS155 2.2 13.6 1.0 NE2 D:HIS214 2.2 12.5 1.0 O D:HOH719 2.3 18.5 1.0 CE1 D:HIS214 3.1 14.1 1.0 CE1 D:HIS155 3.1 15.3 1.0 CD D:GLU267 3.1 14.3 1.0 CD2 D:HIS155 3.2 13.6 1.0 CD2 D:HIS214 3.2 13.2 1.0 OE2 D:GLU267 3.5 14.3 1.0 OH D:TYR257 4.1 15.1 1.0 ND1 D:HIS214 4.2 14.1 1.0 ND1 D:HIS155 4.2 15.2 1.0 O D:HOH822 4.3 30.9 1.0 CG D:HIS155 4.3 12.6 1.0 CG D:HIS214 4.3 13.4 1.0 CG D:GLU267 4.4 14.6 1.0 ND2 D:ASN157 4.4 15.5 1.0 O D:HOH581 4.4 28.4 1.0 CB D:ASN157 4.6 14.1 1.0 CB D:GLU267 4.6 13.5 1.0 CB D:ALA216 4.6 12.3 1.0 CE1 D:TYR257 4.7 13.9 1.0 ND2 D:ASN200 4.7 27.8 1.0 CZ D:TYR257 4.9 14.2 1.0 NE1 D:TRP192 4.9 21.9 1.0 CG D:ASN157 5.0 15.4 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