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Manganese in PDB 3ojn: Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution

Enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution

All present enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution, PDB code: 3ojn was solved by A.J.Fielding, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.77 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.542, 151.497, 96.359, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17.7

Other elements in 3ojn:

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Calcium (Ca) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution (pdb code 3ojn). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution, PDB code: 3ojn:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3ojn

Go back to Manganese Binding Sites List in 3ojn
Manganese binding site 1 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:17.3
occ:1.00
 OE1 A:GLU267 2.1 15.7 1.0
NE2 A:HIS214 2.2 15.6 1.0
O A:HOH1524 2.2 11.6 1.0
O A:HOH1528 2.2 10.8 1.0
NE2 A:HIS155 2.3 15.3 1.0
O A:HOH1519 2.5 16.4 1.0
CE1 A:HIS214 3.1 15.4 1.0
CD A:GLU267 3.2 17.0 1.0
CD2 A:HIS214 3.2 16.6 1.0
CE1 A:HIS155 3.2 16.6 1.0
CD2 A:HIS155 3.3 16.2 1.0
OE2 A:GLU267 3.6 16.3 1.0
NE2 A:HIS200 3.9 16.9 1.0
OH A:TYR257 4.1 15.3 1.0
ND1 A:HIS214 4.2 17.5 1.0
CG A:HIS214 4.3 17.0 1.0
ND1 A:HIS155 4.3 16.2 1.0
ND2 A:ASN157 4.3 17.4 1.0
O A:HOH1537 4.4 18.1 1.0
CG A:HIS155 4.4 16.9 1.0
CG A:GLU267 4.4 13.8 1.0
CB A:GLU267 4.6 14.3 1.0
CB A:ASN157 4.6 17.6 1.0
CE1 A:HIS200 4.6 14.1 1.0
CB A:ALA216 4.6 16.2 1.0
CE1 A:TYR257 4.6 14.6 1.0
CZ A:TYR257 4.8 15.4 1.0
CG A:ASN157 5.0 18.4 1.0

Manganese binding site 2 out of 4 in 3ojn

Go back to Manganese Binding Sites List in 3ojn
Manganese binding site 2 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn500

b:16.1
occ:1.00
 OE1 B:GLU267 2.1 12.5 1.0
O B:HOH1516 2.2 9.1 1.0
O B:HOH1521 2.2 14.2 1.0
NE2 B:HIS214 2.2 13.2 1.0
NE2 B:HIS155 2.3 10.2 1.0
O B:HOH1520 2.3 14.6 1.0
CE1 B:HIS214 3.1 13.1 1.0
CE1 B:HIS155 3.2 12.8 1.0
CD B:GLU267 3.2 15.1 1.0
CD2 B:HIS155 3.2 14.0 1.0
CD2 B:HIS214 3.2 10.8 1.0
OE2 B:GLU267 3.7 16.7 1.0
NE2 B:HIS200 3.9 14.9 1.0
OH B:TYR257 4.1 13.4 1.0
ND1 B:HIS214 4.3 13.6 1.0
ND1 B:HIS155 4.3 12.9 1.0
O B:HOH1530 4.3 17.1 1.0
CG B:HIS214 4.3 12.0 1.0
ND2 B:ASN157 4.3 16.8 1.0
CG B:HIS155 4.4 12.0 1.0
CG B:GLU267 4.5 12.9 1.0
CE1 B:HIS200 4.5 13.8 1.0
CE1 B:TYR257 4.6 12.4 1.0
CB B:GLU267 4.6 13.0 1.0
CB B:ASN157 4.6 14.1 1.0
CB B:ALA216 4.6 11.9 1.0
CZ B:TYR257 4.8 13.4 1.0
CG B:ASN157 5.0 15.3 1.0

Manganese binding site 3 out of 4 in 3ojn

Go back to Manganese Binding Sites List in 3ojn
Manganese binding site 3 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn500

b:14.2
occ:1.00
 OE1 C:GLU267 2.1 12.9 1.0
O C:HOH1518 2.2 9.7 1.0
NE2 C:HIS214 2.2 11.1 1.0
O C:HOH1517 2.2 13.0 1.0
O C:HOH1525 2.3 14.2 1.0
NE2 C:HIS155 2.3 11.7 1.0
CE1 C:HIS214 3.1 13.8 1.0
CE1 C:HIS155 3.1 12.3 1.0
CD C:GLU267 3.2 13.6 1.0
CD2 C:HIS214 3.2 13.8 1.0
CD2 C:HIS155 3.3 11.5 1.0
OE2 C:GLU267 3.6 14.0 1.0
NE2 C:HIS200 3.9 13.7 1.0
OH C:TYR257 4.1 12.7 1.0
ND1 C:HIS214 4.2 12.3 1.0
ND1 C:HIS155 4.3 11.7 1.0
CG C:HIS214 4.3 12.2 1.0
ND2 C:ASN157 4.3 16.1 1.0
O C:HOH1527 4.4 15.1 1.0
CG C:HIS155 4.4 11.8 1.0
CG C:GLU267 4.4 12.9 1.0
CE1 C:HIS200 4.6 11.9 1.0
CB C:GLU267 4.6 11.0 1.0
CE1 C:TYR257 4.6 12.2 1.0
CB C:ASN157 4.6 13.3 1.0
CB C:ALA216 4.6 11.2 1.0
CZ C:TYR257 4.8 13.1 1.0
CG C:ASN157 5.0 14.6 1.0

Manganese binding site 4 out of 4 in 3ojn

Go back to Manganese Binding Sites List in 3ojn
Manganese binding site 4 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn500

b:14.6
occ:1.00
 OE1 D:GLU267 2.1 13.2 1.0
O D:HOH1515 2.2 10.4 1.0
NE2 D:HIS214 2.2 10.4 1.0
O D:HOH1526 2.2 13.3 1.0
O D:HOH1522 2.3 14.3 1.0
NE2 D:HIS155 2.3 10.4 1.0
CE1 D:HIS214 3.1 11.7 1.0
CD D:GLU267 3.2 13.0 1.0
CE1 D:HIS155 3.2 10.6 1.0
CD2 D:HIS214 3.2 12.3 1.0
CD2 D:HIS155 3.3 11.5 1.0
OE2 D:GLU267 3.6 13.3 1.0
NE2 D:HIS200 3.9 12.8 1.0
OH D:TYR257 4.1 14.4 1.0
ND1 D:HIS214 4.2 10.2 1.0
ND2 D:ASN157 4.3 14.2 1.0
ND1 D:HIS155 4.3 12.0 1.0
CG D:HIS214 4.3 9.7 1.0
O D:HOH1529 4.4 16.4 1.0
CG D:HIS155 4.4 10.0 1.0
CG D:GLU267 4.4 11.2 1.0
CE1 D:TYR257 4.5 12.3 1.0
CE1 D:HIS200 4.6 15.1 1.0
CB D:GLU267 4.6 10.2 1.0
CB D:ASN157 4.6 12.7 1.0
CB D:ALA216 4.7 11.3 1.0
CZ D:TYR257 4.8 13.2 1.0
CG D:ASN157 5.0 15.8 1.0

Reference:

A.J.Fielding, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que. A Hyperactive Cobalt-Substituted Extradiol-Cleaving Catechol Dioxygenase. J.Biol.Inorg.Chem. V. 16 341 2011.
ISSN: ISSN 0949-8257
PubMed: 21153851
DOI: 10.1007/S00775-010-0732-0
Page generated: Tue Dec 15 04:13:24 2020

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