Manganese in PDB 1f1u: Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Low Temperature)

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

The structure of Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Low Temperature), PDB code: 1f1u 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 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	137.800, 59.040, 102.250, 90.00, 119.00, 90.00
R / Rfree (%)	16.2 / 18.5

The binding sites of Manganese atom in the Crystal Structure of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis (Native, Low Temperature) (pdb code 1f1u). 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, Low Temperature), PDB code: 1f1u:
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, Low Temperature)


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, Low Temperature) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:16.6 occ:0.40 NE2 A:HIS214 2.0 6.7 1.0 OE1 A:GLU267 2.1 12.2 1.0 O A:HOH1272 2.2 26.4 1.0 NE2 A:HIS155 2.2 6.9 1.0 O A:HOH1271 2.4 10.3 1.0 CE1 A:HIS214 2.8 7.5 1.0 CE1 A:HIS155 3.0 5.4 1.0 CD2 A:HIS214 3.1 6.8 1.0 CD A:GLU267 3.2 9.2 1.0 CD2 A:HIS155 3.3 5.9 1.0 O A:HOH1205 3.5 19.1 1.0 OE2 A:GLU267 3.7 11.0 1.0 OH A:TYR257 3.8 9.6 1.0 NE2 A:HIS200 3.9 5.8 1.0 ND1 A:HIS214 4.0 7.1 1.0 CG A:HIS214 4.2 4.9 1.0 ND1 A:HIS155 4.2 6.0 1.0 CG A:GLU267 4.3 7.5 1.0 CG A:HIS155 4.3 3.5 1.0 CE1 A:HIS200 4.4 5.2 1.0 O A:HOH879 4.4 14.8 1.0 CB A:GLU267 4.4 5.1 1.0 CE1 A:TYR257 4.5 6.2 1.0 ND2 A:ASN157 4.5 7.5 1.0 CB A:ALA216 4.5 5.0 1.0 CZ A:TYR257 4.6 7.6 1.0 CB A:ASN157 4.8 5.8 1.0

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


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, Low Temperature) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn500 b:15.5 occ:0.40 NE2 B:HIS214 2.0 7.7 1.0 OE1 B:GLU267 2.1 11.4 1.0 O B:HOH1274 2.1 28.4 1.0 NE2 B:HIS155 2.2 7.1 1.0 O B:HOH1273 2.4 12.5 1.0 CE1 B:HIS214 2.8 7.4 1.0 CE1 B:HIS155 3.1 5.4 1.0 CD2 B:HIS214 3.2 8.2 1.0 CD B:GLU267 3.2 8.7 1.0 CD2 B:HIS155 3.3 6.0 1.0 O B:HOH1235 3.5 19.1 1.0 OE2 B:GLU267 3.7 10.4 1.0 OH B:TYR257 3.8 10.1 1.0 NE2 B:HIS200 3.9 7.0 1.0 ND1 B:HIS214 4.0 7.3 1.0 CG B:HIS214 4.2 5.1 1.0 ND1 B:HIS155 4.2 6.2 1.0 CG B:HIS155 4.3 5.3 1.0 CE1 B:HIS200 4.3 6.7 1.0 O B:HOH905 4.3 16.1 1.0 CG B:GLU267 4.4 7.6 1.0 CB B:GLU267 4.5 6.5 1.0 CE1 B:TYR257 4.5 7.4 1.0 ND2 B:ASN157 4.5 7.5 1.0 CB B:ALA216 4.5 4.3 1.0 CZ B:TYR257 4.6 8.3 1.0 CB B:ASN157 4.7 6.1 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