Atomistry » Manganese » PDB 3auz-3c5m » 3bza
Atomistry »
  Manganese »
    PDB 3auz-3c5m »
      3bza »

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

Go back to Manganese Binding Sites List in 3bza
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

Go back to Manganese Binding Sites List in 3bza
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: Tue Dec 15 04:08:20 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy