Iron in PDB 1f1x: Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum

All present enzymatic activity of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum:
1.13.11.15;

The structure of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum, PDB code: 1f1x was solved by M.W.Vetting, J.D.Lipscomb, L.P.Wackett, L.Que Jr., D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.60
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	157.100, 157.100, 121.300, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.5

The binding sites of Iron atom in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (pdb code 1f1x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum, PDB code: 1f1x:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:23.4 occ:1.00 FE A:FEL500 0.0 23.4 1.0 OE1 A:GLU267 2.1 18.2 1.0 NE2 A:HIS214 2.1 12.1 1.0 NE2 A:HIS155 2.2 12.6 1.0 O1 A:FEL500 2.2 15.9 1.0 O2 A:FEL500 2.2 28.4 1.0 O3 A:FEL500 2.5 30.9 1.0 CE1 A:HIS214 2.9 15.1 1.0 CE1 A:HIS155 3.1 10.8 1.0 CD A:GLU267 3.2 15.5 1.0 CD2 A:HIS155 3.2 11.5 1.0 CD2 A:HIS214 3.2 13.0 1.0 OE2 A:GLU267 3.7 17.8 1.0 NE2 A:HIS200 3.9 12.3 1.0 OH A:TYR257 4.0 15.7 1.0 ND1 A:HIS214 4.1 12.9 1.0 ND1 A:HIS155 4.2 10.5 1.0 CG A:HIS214 4.3 12.9 1.0 CG A:HIS155 4.3 10.9 1.0 ND2 A:ASN157 4.3 19.0 1.0 CG A:GLU267 4.4 12.8 1.0 CB A:ALA216 4.4 10.1 1.0 CE1 A:HIS200 4.4 12.0 1.0 CB A:GLU267 4.4 11.4 1.0 CE1 A:TYR257 4.6 12.2 1.0 CB A:ASN157 4.7 12.4 1.0 CZ A:TYR257 4.8 13.4 1.0 O A:HOH1320 4.8 29.9 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:23.1 occ:1.00 FE B:FEL500 0.0 23.1 1.0 NE2 B:HIS214 2.1 9.4 1.0 OE1 B:GLU267 2.1 16.6 1.0 O3 B:FEL500 2.2 27.9 1.0 NE2 B:HIS155 2.2 12.2 1.0 O1 B:FEL500 2.2 15.8 1.0 O2 B:FEL500 2.4 26.7 1.0 CE1 B:HIS214 3.0 13.9 1.0 CE1 B:HIS155 3.1 11.9 1.0 CD B:GLU267 3.2 16.3 1.0 CD2 B:HIS214 3.2 11.8 1.0 CD2 B:HIS155 3.3 12.1 1.0 OE2 B:GLU267 3.7 16.9 1.0 NE2 B:HIS200 3.9 13.6 1.0 OH B:TYR257 3.9 14.7 1.0 O B:HOH1675 4.0 36.7 1.0 ND1 B:HIS214 4.1 11.2 1.0 ND1 B:HIS155 4.2 12.1 1.0 CG B:HIS214 4.3 10.7 1.0 CG B:HIS155 4.3 10.0 1.0 CE1 B:HIS200 4.4 14.0 1.0 CG B:GLU267 4.4 13.8 1.0 CB B:ALA216 4.5 12.0 1.0 ND2 B:ASN157 4.5 18.1 1.0 CB B:GLU267 4.5 13.4 1.0 CE1 B:TYR257 4.6 11.9 1.0 CZ B:TYR257 4.7 13.5 1.0 CB B:ASN157 4.7 14.6 1.0 O B:HOH1568 4.8 30.9 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:22.7 occ:1.00 FE C:FEL500 0.0 22.7 1.0 OE1 C:GLU267 2.0 17.9 1.0 NE2 C:HIS214 2.1 13.2 1.0 O2 C:FEL500 2.2 25.8 1.0 NE2 C:HIS155 2.2 12.0 1.0 O1 C:FEL500 2.3 17.1 1.0 O3 C:FEL500 2.5 30.1 1.0 CE1 C:HIS214 2.8 14.6 1.0 CE1 C:HIS155 3.1 12.4 1.0 CD C:GLU267 3.1 16.9 1.0 CD2 C:HIS214 3.2 13.6 1.0 CD2 C:HIS155 3.3 11.2 1.0 OE2 C:GLU267 3.6 16.9 1.0 OH C:TYR257 3.8 14.7 1.0 O C:HOH1450 3.9 33.6 1.0 NE2 C:HIS200 4.0 13.4 1.0 ND1 C:HIS214 4.0 11.9 1.0 CG C:HIS214 4.2 11.5 1.0 ND1 C:HIS155 4.2 11.1 1.0 CG C:HIS155 4.4 11.6 1.0 CG C:GLU267 4.4 13.5 1.0 CB C:ALA216 4.4 10.3 1.0 ND2 C:ASN157 4.4 18.2 1.0 CB C:GLU267 4.5 12.3 1.0 CE1 C:TYR257 4.5 10.4 1.0 CE1 C:HIS200 4.5 13.0 1.0 CB C:ASN157 4.7 13.6 1.0 CZ C:TYR257 4.7 11.2 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:23.8 occ:1.00 FE D:FEL500 0.0 23.8 1.0 OE1 D:GLU267 2.0 17.2 1.0 O2 D:FEL500 2.1 23.1 1.0 NE2 D:HIS214 2.1 10.9 1.0 NE2 D:HIS155 2.2 12.3 1.0 O1 D:FEL500 2.3 15.6 1.0 O3 D:FEL500 2.4 27.9 1.0 CE1 D:HIS214 2.9 13.1 1.0 CE1 D:HIS155 3.1 12.6 1.0 CD D:GLU267 3.1 16.1 1.0 CD2 D:HIS214 3.2 13.2 1.0 CD2 D:HIS155 3.2 13.5 1.0 OE2 D:GLU267 3.6 18.4 1.0 NE2 D:HIS200 3.9 13.6 1.0 OH D:TYR257 4.0 13.9 1.0 ND1 D:HIS214 4.1 12.1 1.0 ND1 D:HIS155 4.2 10.8 1.0 CG D:HIS214 4.2 11.3 1.0 CG D:HIS155 4.3 11.1 1.0 CG D:GLU267 4.3 11.9 1.0 CE1 D:HIS200 4.4 14.2 1.0 ND2 D:ASN157 4.4 16.7 1.0 CB D:ALA216 4.4 12.0 1.0 CB D:GLU267 4.4 11.6 1.0 CE2 D:TYR257 4.5 12.7 1.0 CB D:ASN157 4.7 14.8 1.0 CZ D:TYR257 4.7 13.5 1.0

M.W.Vetting, L.P.Wackett, L.Que Jr., J.D.Lipscomb, D.H.Ohlendorf. Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases. J.Bacteriol. V. 186 1945 2004.
ISSN: ISSN 0021-9193
PubMed: 15028678
DOI: 10.1128/JB.186.7.1945-1958.2004