Manganese in PDB 1f1r: Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo)

All present enzymatic activity of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo):
1.13.11.15;

The structure of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo), PDB code: 1f1r 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)	20.00 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	138.440, 59.150, 102.800, 90.00, 118.26, 90.00
R / Rfree (%)	15.6 / 18.7

The binding sites of Manganese atom in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo) (pdb code 1f1r). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo), PDB code: 1f1r:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:14.4 occ:0.50 OE1 A:GLU267 2.0 12.2 1.0 O A:HOH946 2.0 24.9 1.0 NE2 A:HIS214 2.1 7.0 1.0 NE2 A:HIS155 2.2 6.0 1.0 O A:HOH945 2.3 11.8 1.0 O A:HOH947 2.7 31.4 1.0 CE1 A:HIS214 3.0 6.4 1.0 CE1 A:HIS155 3.0 7.5 1.0 CD A:GLU267 3.1 12.9 1.0 CD2 A:HIS214 3.1 7.4 1.0 CD2 A:HIS155 3.2 7.1 1.0 OE2 A:GLU267 3.6 15.0 1.0 NE2 A:HIS200 3.9 7.9 1.0 OH A:TYR257 3.9 10.4 1.0 ND1 A:HIS214 4.1 7.0 1.0 ND1 A:HIS155 4.2 7.5 1.0 CG A:HIS214 4.2 6.0 1.0 CG A:HIS155 4.3 7.5 1.0 CG A:GLU267 4.3 9.8 1.0 CE1 A:HIS200 4.4 8.5 1.0 CB A:GLU267 4.4 5.9 1.0 CB A:ALA216 4.5 6.2 1.0 ND2 A:ASN157 4.5 13.9 1.0 CE1 A:TYR257 4.6 7.2 1.0 CZ A:TYR257 4.7 9.5 1.0 CB A:ASN157 4.8 8.7 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Non-Cryo) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn500 b:15.4 occ:0.50 OE1 B:GLU267 2.0 11.6 1.0 O B:HOH949 2.1 27.7 1.0 NE2 B:HIS214 2.2 7.9 1.0 O B:HOH948 2.2 12.9 1.0 NE2 B:HIS155 2.2 6.2 1.0 O B:HOH950 2.6 41.2 1.0 CE1 B:HIS214 3.0 7.7 1.0 CE1 B:HIS155 3.1 7.5 1.0 CD B:GLU267 3.1 10.4 1.0 CD2 B:HIS155 3.2 6.8 1.0 CD2 B:HIS214 3.3 8.3 1.0 OE2 B:GLU267 3.5 13.1 1.0 NE2 B:HIS200 3.8 5.9 1.0 OH B:TYR257 3.9 11.1 1.0 ND1 B:HIS214 4.2 8.4 1.0 ND1 B:HIS155 4.2 7.6 1.0 CE1 B:HIS200 4.3 6.9 1.0 CG B:HIS214 4.3 6.7 1.0 CG B:HIS155 4.3 6.2 1.0 CG B:GLU267 4.3 8.0 1.0 ND2 B:ASN157 4.4 10.7 1.0 CB B:GLU267 4.5 6.4 1.0 CB B:ALA216 4.6 6.5 1.0 CE2 B:TYR257 4.6 8.1 1.0 CZ B:TYR257 4.7 10.0 1.0 CB B:ASN157 4.9 8.0 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