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Manganese in PDB 1f1v: Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate)

Enzymatic activity of Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate)

All present enzymatic activity of Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate):
1.13.11.15;

Protein crystallography data

The structure of Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate), PDB code: 1f1v 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 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 139.420, 59.300, 103.200, 90.00, 118.39, 90.00
R / Rfree (%) 16.6 / 20

Manganese Binding Sites:

The binding sites of Manganese atom in the Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate) (pdb code 1f1v). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate), PDB code: 1f1v:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1f1v

Go back to Manganese Binding Sites List in 1f1v
Manganese binding site 1 out of 2 in the Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:19.3
occ:1.00
 O3 A:DHY999 1.9 28.9 1.0
OE1 A:GLU267 2.0 16.7 1.0
NE2 A:HIS155 2.1 14.9 1.0
O4 A:DHY999 2.1 28.2 1.0
NE2 A:HIS214 2.2 16.7 1.0
O A:HOH915 2.3 21.6 1.0
C3 A:DHY999 2.9 28.6 1.0
CE1 A:HIS155 3.0 16.6 1.0
C4 A:DHY999 3.0 28.8 1.0
CE1 A:HIS214 3.1 18.4 1.0
CD A:GLU267 3.1 19.0 1.0
CD2 A:HIS155 3.2 13.7 1.0
CD2 A:HIS214 3.2 17.6 1.0
OE2 A:GLU267 3.5 18.6 1.0
OH A:TYR257 3.9 19.5 1.0
NE2 A:HIS200 3.9 17.1 1.0
ND1 A:HIS155 4.2 12.8 1.0
ND1 A:HIS214 4.2 17.2 1.0
CG A:HIS155 4.3 14.2 1.0
C2 A:DHY999 4.3 28.8 1.0
CG A:HIS214 4.3 17.1 1.0
CG A:GLU267 4.4 16.5 1.0
C5 A:DHY999 4.4 29.4 1.0
CB A:ALA216 4.5 14.1 1.0
CB A:GLU267 4.6 16.3 1.0
CE1 A:TYR257 4.6 14.9 1.0
CE1 A:HIS200 4.6 18.3 1.0
ND2 A:ASN157 4.6 22.1 1.0
CZ A:TYR257 4.7 17.4 1.0
CB A:ASN157 4.8 19.0 1.0
CD2 A:TYR269 4.9 29.1 1.0
CE2 A:TYR269 5.0 30.4 1.0

Manganese binding site 2 out of 2 in 1f1v

Go back to Manganese Binding Sites List in 1f1v
Manganese binding site 2 out of 2 in the Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Anaerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Arthrobacter Globiformis. (Complex with 3,4- Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn500

b:17.9
occ:1.00
 OE1 B:GLU267 2.0 17.1 1.0
O4 B:DHY999 2.0 26.4 1.0
O3 B:DHY999 2.0 27.6 1.0
NE2 B:HIS155 2.2 13.8 1.0
NE2 B:HIS214 2.2 11.9 1.0
O B:HOH916 2.2 23.2 1.0
C3 B:DHY999 3.0 28.4 1.0
C4 B:DHY999 3.0 27.8 1.0
CE1 B:HIS155 3.0 16.5 1.0
CE1 B:HIS214 3.1 14.5 1.0
CD B:GLU267 3.1 18.4 1.0
CD2 B:HIS155 3.3 14.5 1.0
CD2 B:HIS214 3.3 13.5 1.0
OE2 B:GLU267 3.6 20.3 1.0
NE2 B:HIS200 4.0 16.7 1.0
OH B:TYR257 4.0 18.4 1.0
ND1 B:HIS155 4.2 12.9 1.0
ND1 B:HIS214 4.2 14.7 1.0
CG B:GLU267 4.3 17.2 1.0
CG B:HIS155 4.3 13.5 1.0
C2 B:DHY999 4.3 28.7 1.0
C5 B:DHY999 4.4 27.4 1.0
CG B:HIS214 4.4 14.2 1.0
ND2 B:ASN157 4.4 23.1 1.0
CE1 B:TYR257 4.5 15.7 1.0
CB B:ALA216 4.5 14.3 1.0
CB B:GLU267 4.5 15.6 1.0
CE1 B:HIS200 4.6 16.2 1.0
CZ B:TYR257 4.7 17.6 1.0
CB B:ASN157 4.9 18.1 1.0
CD2 B:TYR269 4.9 28.2 1.0
CE2 B:TYR269 4.9 30.1 1.0
NE2 B:HIS248 5.0 24.5 1.0

Reference:

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
Page generated: Sat Oct 5 10:14:02 2024

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