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Chlorine 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:

Manganese (Mn) 4 atoms
Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 4 binding sites of Chlorine 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 Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3bza

Go back to Chlorine Binding Sites List in 3bza
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl501

b:19.0
occ:1.00
 NH1 A:ARG243 3.2 18.2 1.0
NH1 A:ARG293 3.2 15.5 1.0
O A:HOH750 3.2 23.6 1.0
NH2 A:ARG243 3.3 16.5 1.0
CE1 A:HIS248 3.3 17.2 1.0
ND1 A:HIS248 3.4 16.4 1.0
CG A:ARG293 3.5 15.1 1.0
CB A:ARG293 3.5 16.6 1.0
O A:ARG293 3.7 16.6 1.0
CZ A:ARG243 3.7 17.2 1.0
CD A:ARG293 3.7 16.5 1.0
CA A:ARG293 3.8 15.6 1.0
OH A:TYR257 3.9 17.0 1.0
C A:ARG293 4.1 16.3 1.0
CH2 A:TRP304 4.2 20.0 1.0
CZ2 A:TRP304 4.2 18.1 1.0
CZ A:ARG293 4.3 16.8 1.0
O A:HOH504 4.3 8.4 0.3
NE A:ARG293 4.4 15.9 1.0
NE2 A:HIS248 4.4 17.3 1.0
O A:HOH504 4.6 15.9 0.7
CG A:HIS248 4.6 15.1 1.0
CZ3 A:TRP304 4.8 19.3 1.0
CZ A:TYR257 4.9 14.3 1.0
CE2 A:TRP304 4.9 16.4 1.0

Chlorine binding site 2 out of 4 in 3bza

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl502

b:18.1
occ:1.00
 O B:HOH1017 3.1 22.7 1.0
NH1 B:ARG243 3.2 16.2 1.0
CE1 B:HIS248 3.3 15.8 1.0
NH2 B:ARG243 3.3 15.7 1.0
NH1 B:ARG293 3.3 16.4 1.0
ND1 B:HIS248 3.4 13.8 1.0
CB B:ARG293 3.4 14.5 1.0
CG B:ARG293 3.5 15.5 1.0
CD B:ARG293 3.6 14.6 1.0
CZ B:ARG243 3.7 15.6 1.0
O B:ARG293 3.7 15.4 1.0
CA B:ARG293 3.8 14.6 1.0
OH B:TYR257 4.0 15.7 1.0
C B:ARG293 4.1 15.2 1.0
O B:HOH758 4.2 10.2 0.3
CH2 B:TRP304 4.3 18.1 1.0
CZ B:ARG293 4.3 16.6 1.0
CZ2 B:TRP304 4.3 20.2 1.0
NE B:ARG293 4.4 16.0 1.0
NE2 B:HIS248 4.4 13.9 1.0
O B:HOH758 4.5 13.5 0.7
CG B:HIS248 4.6 14.7 1.0
CZ B:TYR257 4.9 14.4 1.0
CZ3 B:TRP304 4.9 18.7 1.0
CE2 B:TRP304 5.0 17.7 1.0

Chlorine binding site 3 out of 4 in 3bza

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl501

b:22.9
occ:1.00
 NH1 C:ARG243 3.2 20.2 1.0
NH1 C:ARG293 3.2 19.6 1.0
O C:HOH723 3.3 27.9 1.0
NH2 C:ARG243 3.3 19.9 1.0
CE1 C:HIS248 3.3 19.2 1.0
ND1 C:HIS248 3.3 16.3 1.0
CB C:ARG293 3.6 18.6 1.0
CD C:ARG293 3.6 19.1 1.0
CZ C:ARG243 3.7 18.7 1.0
CG C:ARG293 3.7 19.4 1.0
O C:ARG293 3.8 19.9 1.0
CA C:ARG293 3.8 19.1 1.0
OH C:TYR257 3.9 17.7 1.0
CH2 C:TRP304 4.1 21.3 1.0
C C:ARG293 4.1 18.8 1.0
CZ2 C:TRP304 4.2 21.2 1.0
CZ C:ARG293 4.2 19.0 1.0
NE C:ARG293 4.4 17.8 1.0
O C:HOH504 4.4 12.1 0.3
NE2 C:HIS248 4.4 16.9 1.0
CG C:HIS248 4.6 16.7 1.0
O C:HOH504 4.7 16.6 0.7
CZ3 C:TRP304 4.7 21.8 1.0
CE2 C:TRP304 4.9 20.6 1.0
CZ C:TYR257 4.9 16.1 1.0

Chlorine binding site 4 out of 4 in 3bza

Go back to Chlorine Binding Sites List in 3bza
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl501

b:20.4
occ:1.00
 NH1 D:ARG243 3.2 16.7 1.0
O D:HOH913 3.2 30.3 1.0
CE1 D:HIS248 3.2 16.4 1.0
NH2 D:ARG243 3.3 15.0 1.0
NH1 D:ARG293 3.3 17.1 1.0
ND1 D:HIS248 3.4 15.4 1.0
CB D:ARG293 3.5 15.2 1.0
CG D:ARG293 3.6 16.6 1.0
CZ D:ARG243 3.7 15.9 1.0
CD D:ARG293 3.7 17.0 1.0
O D:ARG293 3.8 15.9 1.0
CA D:ARG293 3.8 15.1 1.0
OH D:TYR257 3.9 15.0 1.0
CH2 D:TRP304 4.1 18.7 1.0
C D:ARG293 4.1 15.2 1.0
CZ2 D:TRP304 4.2 20.4 1.0
CZ D:ARG293 4.3 17.8 1.0
NE2 D:HIS248 4.4 15.3 1.0
O D:HOH671 4.4 12.6 0.3
NE D:ARG293 4.5 18.4 1.0
O D:HOH671 4.5 16.4 0.7
CG D:HIS248 4.6 15.2 1.0
CZ3 D:TRP304 4.7 19.3 1.0
CZ D:TYR257 4.9 15.1 1.0
CE2 D:TRP304 4.9 17.4 1.0
CE2 D:TYR257 5.0 15.8 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 Dec 12 09:33:57 2020

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