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Chlorine in PDB 3ojj: Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution

Enzymatic activity of Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution

All present enzymatic activity of Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution, PDB code: 3ojj 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) 29.62 / 1.72
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.539, 152.075, 96.491, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 17.6

Other elements in 3ojj:

The structure of Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution also contains other interesting chemical elements:

Cobalt (Co) 4 atoms
Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution (pdb code 3ojj). 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 Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution, PDB code: 3ojj:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3ojj

Go back to Chlorine Binding Sites List in 3ojj
Chlorine binding site 1 out of 4 in the Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 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 Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl367

b:16.1
occ:1.00
 NH1 A:ARG243 3.2 13.7 1.0
O A:HOH658 3.2 19.4 1.0
NH2 A:ARG243 3.2 12.1 1.0
CE1 A:HIS248 3.2 14.2 1.0
NH1 A:ARG293 3.3 12.8 1.0
ND1 A:HIS248 3.3 12.2 1.0
CB A:ARG293 3.4 12.1 1.0
CG A:ARG293 3.5 11.2 1.0
CD A:ARG293 3.6 12.7 1.0
CZ A:ARG243 3.6 14.7 1.0
CA A:ARG293 3.7 12.2 1.0
O A:ARG293 3.7 12.7 1.0
OH A:TYR257 3.9 12.4 1.0
C A:ARG293 4.0 11.3 1.0
CH2 A:TRP304 4.1 15.8 1.0
CZ2 A:TRP304 4.2 14.5 1.0
CZ A:ARG293 4.3 14.1 1.0
NE2 A:HIS248 4.4 13.2 1.0
NE A:ARG293 4.4 12.4 1.0
CG A:HIS248 4.6 10.5 1.0
O A:HOH650 4.6 11.7 1.0
CZ3 A:TRP304 4.8 15.0 1.0
CZ A:TYR257 5.0 10.4 1.0
NE A:ARG243 5.0 11.2 1.0

Chlorine binding site 2 out of 4 in 3ojj

Go back to Chlorine Binding Sites List in 3ojj
Chlorine binding site 2 out of 4 in the Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 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 Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl370

b:13.0
occ:1.00
 NH1 B:ARG243 3.2 11.3 1.0
CE1 B:HIS248 3.2 11.3 1.0
O B:HOH692 3.2 16.4 1.0
NH1 B:ARG293 3.2 13.9 1.0
NH2 B:ARG243 3.3 13.0 1.0
ND1 B:HIS248 3.3 11.8 1.0
CB B:ARG293 3.4 12.0 1.0
CG B:ARG293 3.6 12.5 1.0
CD B:ARG293 3.7 13.0 1.0
CZ B:ARG243 3.7 11.9 1.0
CA B:ARG293 3.8 11.7 1.0
O B:ARG293 3.8 11.3 1.0
OH B:TYR257 3.9 11.1 1.0
C B:ARG293 4.1 11.1 1.0
CH2 B:TRP304 4.1 14.2 1.0
CZ2 B:TRP304 4.2 16.1 1.0
CZ B:ARG293 4.3 12.2 1.0
NE2 B:HIS248 4.4 10.0 1.0
NE B:ARG293 4.4 13.3 1.0
CG B:HIS248 4.5 8.9 1.0
O B:HOH690 4.6 11.2 1.0
CZ3 B:TRP304 4.8 16.2 1.0
CZ B:TYR257 4.9 10.9 1.0
CE2 B:TRP304 5.0 13.8 1.0

Chlorine binding site 3 out of 4 in 3ojj

Go back to Chlorine Binding Sites List in 3ojj
Chlorine binding site 3 out of 4 in the Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 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 Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl368

b:16.2
occ:1.00
 NH1 C:ARG293 3.2 15.3 1.0
NH1 C:ARG243 3.2 17.1 1.0
CE1 C:HIS248 3.2 13.5 1.0
NH2 C:ARG243 3.3 15.7 1.0
O C:HOH642 3.3 17.2 1.0
ND1 C:HIS248 3.3 15.4 1.0
CB C:ARG293 3.5 14.5 1.0
CG C:ARG293 3.6 17.2 1.0
CD C:ARG293 3.7 15.2 1.0
CZ C:ARG243 3.7 15.7 1.0
O C:ARG293 3.8 14.6 1.0
CA C:ARG293 3.8 14.5 1.0
OH C:TYR257 4.0 12.3 1.0
C C:ARG293 4.1 14.6 1.0
CH2 C:TRP304 4.1 17.7 1.0
CZ C:ARG293 4.2 13.8 1.0
CZ2 C:TRP304 4.3 17.1 1.0
NE2 C:HIS248 4.3 13.6 1.0
NE C:ARG293 4.4 16.0 1.0
CG C:HIS248 4.6 13.1 1.0
O C:HOH638 4.6 12.6 1.0
CZ3 C:TRP304 4.8 17.7 1.0
CZ C:TYR257 5.0 12.0 1.0

Chlorine binding site 4 out of 4 in 3ojj

Go back to Chlorine Binding Sites List in 3ojj
Chlorine binding site 4 out of 4 in the Structure of Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 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 Co-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.72 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl367

b:14.7
occ:1.00
 O D:HOH678 3.2 20.7 1.0
CE1 D:HIS248 3.2 9.2 1.0
NH1 D:ARG293 3.2 14.6 1.0
NH2 D:ARG243 3.3 12.4 1.0
NH1 D:ARG243 3.3 14.3 1.0
ND1 D:HIS248 3.3 10.3 1.0
CB D:ARG293 3.5 11.2 1.0
CG D:ARG293 3.6 11.7 1.0
CD D:ARG293 3.7 10.5 1.0
O D:ARG293 3.7 11.0 1.0
CZ D:ARG243 3.8 11.4 1.0
CA D:ARG293 3.8 10.8 1.0
OH D:TYR257 3.9 11.4 1.0
C D:ARG293 4.1 10.8 1.0
CH2 D:TRP304 4.1 14.8 1.0
CZ2 D:TRP304 4.2 15.7 1.0
CZ D:ARG293 4.3 11.4 1.0
NE2 D:HIS248 4.4 8.9 1.0
NE D:ARG293 4.4 12.8 1.0
CG D:HIS248 4.6 9.4 1.0
O D:HOH674 4.6 10.5 1.0
CZ3 D:TRP304 4.8 16.6 1.0
CZ D:TYR257 4.9 10.9 1.0
CE2 D:TRP304 5.0 13.1 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: Sun Jul 21 01:42:22 2024

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