Iron in PDB 1q0o: Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein)

All present enzymatic activity of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein):
1.13.11.15;

The structure of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein), PDB code: 1q0o was solved by M.W.Vetting, L.P.Wackett, L.Que, J.D.Lipscomb, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.900, 118.900, 110.300, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 20.8

The binding sites of Iron atom in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein) (pdb code 1q0o). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein), PDB code: 1q0o:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein)


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 (Full Length Protein) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:19.9 occ:1.00 O A:HOH591 1.9 22.4 1.0 OE1 A:GLU267 2.0 17.0 1.0 NE2 A:HIS155 2.2 7.2 1.0 NE2 A:HIS214 2.3 7.1 1.0 O A:HOH589 2.6 15.1 1.0 O A:HOH590 3.0 12.9 1.0 CE1 A:HIS214 3.1 6.3 1.0 CE1 A:HIS155 3.1 7.0 1.0 CD A:GLU267 3.1 11.6 1.0 CD2 A:HIS155 3.2 5.7 1.0 CD2 A:HIS214 3.4 7.7 1.0 OE2 A:GLU267 3.5 9.6 1.0 NE2 A:HIS200 3.8 9.5 1.0 OH A:TYR257 4.1 9.9 1.0 ND1 A:HIS155 4.2 5.9 1.0 ND1 A:HIS214 4.2 6.9 1.0 CG A:HIS155 4.3 5.2 1.0 CG A:GLU267 4.4 6.0 1.0 CG A:HIS214 4.4 9.0 1.0 CE1 A:HIS200 4.5 10.5 1.0 ND2 A:ASN157 4.5 16.6 1.0 CE1 A:TYR257 4.6 5.5 1.0 CB A:GLU267 4.6 5.8 1.0 CB A:ALA216 4.7 4.7 1.0 CB A:ASN157 4.7 11.3 1.0 CZ A:TYR257 4.8 6.9 1.0 CD2 A:TYR269 4.9 19.2 1.0 CD2 A:HIS200 4.9 10.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum (Full Length Protein)


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 (Full Length Protein) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:14.4 occ:1.00 OE1 B:GLU267 1.9 11.9 1.0 NE2 B:HIS155 2.2 4.6 1.0 O B:HOH604 2.3 25.3 1.0 NE2 B:HIS214 2.4 5.0 1.0 O B:HOH600 3.0 7.5 1.0 CD B:GLU267 3.0 9.9 1.0 CE1 B:HIS214 3.1 4.3 1.0 CE1 B:HIS155 3.1 5.5 1.0 CD2 B:HIS155 3.2 6.3 1.0 CD2 B:HIS214 3.5 4.0 1.0 OE2 B:GLU267 3.5 11.6 1.0 O B:HOH601 3.8 26.7 1.0 OH B:TYR257 3.8 3.5 1.0 NE2 B:HIS200 3.9 10.1 1.0 ND1 B:HIS155 4.2 6.5 1.0 ND1 B:HIS214 4.3 4.7 1.0 CG B:HIS155 4.3 4.3 1.0 ND2 B:ASN157 4.3 10.3 1.0 CG B:GLU267 4.3 8.6 1.0 CG B:HIS214 4.5 6.4 1.0 CE1 B:HIS200 4.5 9.3 1.0 CE1 B:TYR257 4.5 3.7 1.0 CB B:GLU267 4.6 6.1 1.0 CB B:ALA216 4.6 6.3 1.0 CZ B:TYR257 4.6 3.8 1.0 CB B:ASN157 4.8 8.8 1.0 CD2 B:TYR269 4.9 17.1 1.0

M.W.Vetting, L.P.Wackett, L.Que, 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