Atomistry » Manganese » PDB 1en6-1g0i » 1f1v
Atomistry »
  Manganese »
    PDB 1en6-1g0i »
      1f1v »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy