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Manganese in PDB 3bza: Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution

Enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution

All present enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution, PDB code: 3bza was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.82 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.502, 152.191, 96.278, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 19.7

Other elements in 3bza:

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 From B.Fuscum at 1.7 Ang Resolution (pdb code 3bza). 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 From B.Fuscum at 1.7 Ang Resolution, PDB code: 3bza:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3bza

Go back to Manganese Binding Sites List in 3bza
Manganese binding site 1 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 From B.Fuscum at 1.7 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:20.3
occ:1.00
 OE1 A:GLU267 2.1 17.9 1.0
O A:HOH503 2.2 15.8 1.0
O A:HOH505 2.2 18.4 1.0
NE2 A:HIS214 2.3 17.2 1.0
NE2 A:HIS155 2.3 15.4 1.0
O A:HOH504 2.3 15.9 0.7
CE1 A:HIS214 3.1 17.2 1.0
CD A:GLU267 3.2 18.0 1.0
CE1 A:HIS155 3.2 14.7 1.0
CD2 A:HIS155 3.3 16.1 1.0
CD2 A:HIS214 3.3 19.4 1.0
O A:HOH504 3.4 8.4 0.3
OE2 A:GLU267 3.6 18.3 1.0
NE2 A:HIS200 3.8 17.5 1.0
OH A:TYR257 4.1 17.0 1.0
ND1 A:HIS214 4.3 17.1 1.0
ND2 A:ASN157 4.3 17.5 1.0
ND1 A:HIS155 4.3 15.1 1.0
O A:HOH749 4.3 21.1 1.0
CG A:HIS155 4.4 15.2 1.0
CG A:HIS214 4.4 17.7 1.0
CG A:GLU267 4.5 17.0 1.0
CE1 A:HIS200 4.5 16.2 1.0
CE1 A:TYR257 4.5 16.1 1.0
CB A:GLU267 4.6 16.4 1.0
CB A:ASN157 4.6 16.2 1.0
CB A:ALA216 4.6 17.2 1.0
CZ A:TYR257 4.8 14.3 1.0
CD2 A:HIS200 5.0 17.6 1.0
CD1 A:TYR269 5.0 15.1 1.0
CG A:ASN157 5.0 17.9 1.0

Manganese binding site 2 out of 4 in 3bza

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Manganese binding site 2 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 From B.Fuscum at 1.7 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn500

b:17.4
occ:1.00
 OE1 B:GLU267 2.0 14.9 1.0
O B:HOH757 2.1 13.0 1.0
NE2 B:HIS155 2.2 14.8 1.0
NE2 B:HIS214 2.2 14.4 1.0
O B:HOH759 2.3 22.5 1.0
O B:HOH758 2.4 13.5 0.7
CE1 B:HIS214 3.0 13.9 1.0
CE1 B:HIS155 3.1 14.7 1.0
CD B:GLU267 3.1 15.4 1.0
CD2 B:HIS155 3.2 16.4 1.0
CD2 B:HIS214 3.3 15.6 1.0
O B:HOH758 3.4 10.2 0.3
OE2 B:GLU267 3.6 14.7 1.0
NE2 B:HIS200 3.8 16.9 1.0
OH B:TYR257 4.1 15.7 1.0
ND1 B:HIS214 4.2 14.2 1.0
ND1 B:HIS155 4.2 14.7 1.0
CG B:HIS155 4.3 14.7 1.0
CG B:HIS214 4.4 14.5 1.0
CG B:GLU267 4.4 12.5 1.0
O B:HOH1016 4.4 19.1 1.0
ND2 B:ASN157 4.4 15.2 1.0
CE1 B:HIS200 4.5 16.5 1.0
CE1 B:TYR257 4.5 14.1 1.0
CB B:GLU267 4.5 14.0 1.0
CB B:ASN157 4.6 14.8 1.0
CB B:ALA216 4.7 15.9 1.0
CZ B:TYR257 4.8 14.4 1.0
CD2 B:HIS200 5.0 17.2 1.0

Manganese binding site 3 out of 4 in 3bza

Go back to Manganese Binding Sites List in 3bza
Manganese binding site 3 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 From B.Fuscum at 1.7 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn500

b:21.0
occ:1.00
 OE1 C:GLU267 2.1 18.0 1.0
O C:HOH503 2.2 16.6 1.0
NE2 C:HIS214 2.2 15.9 1.0
O C:HOH504 2.3 16.6 0.7
NE2 C:HIS155 2.3 15.4 1.0
O C:HOH505 2.3 22.4 1.0
CE1 C:HIS214 3.0 15.6 1.0
CE1 C:HIS155 3.2 15.3 1.0
CD C:GLU267 3.2 17.4 1.0
CD2 C:HIS155 3.3 15.5 1.0
CD2 C:HIS214 3.3 19.0 1.0
O C:HOH504 3.5 12.1 0.3
OE2 C:GLU267 3.7 19.9 1.0
NE2 C:HIS200 3.8 20.0 1.0
OH C:TYR257 4.1 17.7 1.0
ND1 C:HIS214 4.2 16.5 1.0
ND1 C:HIS155 4.3 13.8 1.0
CG C:HIS214 4.3 16.8 1.0
O C:HOH717 4.4 21.5 1.0
CG C:HIS155 4.4 15.7 1.0
ND2 C:ASN157 4.4 16.6 1.0
CG C:GLU267 4.4 14.2 1.0
CB C:GLU267 4.5 14.3 1.0
CE1 C:HIS200 4.5 20.3 1.0
CB C:ASN157 4.6 17.9 1.0
CE1 C:TYR257 4.6 14.4 1.0
CB C:ALA216 4.6 16.1 1.0
CZ C:TYR257 4.8 16.1 1.0
CD1 C:TYR269 4.9 19.1 1.0
CD2 C:HIS200 4.9 20.2 1.0
CG C:ASN157 5.0 17.8 1.0

Manganese binding site 4 out of 4 in 3bza

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Manganese binding site 4 out of 4 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 From B.Fuscum at 1.7 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn500

b:19.4
occ:1.00
 OE1 D:GLU267 2.0 15.9 1.0
NE2 D:HIS214 2.2 15.9 1.0
O D:HOH670 2.2 18.1 1.0
NE2 D:HIS155 2.3 16.1 1.0
O D:HOH672 2.3 21.9 1.0
O D:HOH671 2.3 16.4 0.7
CE1 D:HIS214 3.1 18.4 1.0
CE1 D:HIS155 3.1 13.4 1.0
CD D:GLU267 3.1 17.7 1.0
CD2 D:HIS214 3.2 18.7 1.0
CD2 D:HIS155 3.3 14.6 1.0
O D:HOH671 3.5 12.6 0.3
OE2 D:GLU267 3.6 19.8 1.0
NE2 D:HIS200 3.9 19.5 1.0
OH D:TYR257 4.0 15.0 1.0
ND1 D:HIS214 4.2 16.2 1.0
ND1 D:HIS155 4.3 16.8 1.0
CG D:HIS214 4.3 15.9 1.0
CG D:HIS155 4.4 15.8 1.0
ND2 D:ASN157 4.4 16.3 1.0
CG D:GLU267 4.4 16.6 1.0
O D:HOH940 4.4 19.9 1.0
CE1 D:TYR257 4.5 15.3 1.0
CE1 D:HIS200 4.6 18.4 1.0
CB D:GLU267 4.6 15.0 1.0
CB D:ASN157 4.6 16.7 1.0
CB D:ALA216 4.7 16.1 1.0
CZ D:TYR257 4.7 15.1 1.0
CD2 D:HIS200 4.9 19.2 1.0
CD1 D:TYR269 5.0 15.8 1.0
CG D:ASN157 5.0 18.2 1.0

Reference:

J.P.Emerson, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que. Swapping Metals in Fe- and Mn-Dependent Dioxygenases: Evidence For Oxygen Activation Without A Change in Metal Redox State. Proc.Natl.Acad.Sci.Usa V. 105 7347 2008.
ISSN: ISSN 0027-8424
PubMed: 18492808
DOI: 10.1073/PNAS.0711179105
Page generated: Sat Oct 5 15:59:20 2024

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