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Chlorine in PDB 3ecj: Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution

Enzymatic activity of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution

All present enzymatic activity of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution, PDB code: 3ecj 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) 23.46 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.711, 163.403, 101.584, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 19.4

Other elements in 3ecj:

The structure of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution (pdb code 3ecj). 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution, PDB code: 3ecj:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3ecj

Go back to Chlorine Binding Sites List in 3ecj
Chlorine binding site 1 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:18.0
occ:1.00
 O A:HOH811 3.1 27.6 1.0
NH1 A:ARG293 3.2 15.0 1.0
NH1 A:ARG243 3.3 15.1 1.0
NH2 A:ARG243 3.3 13.5 1.0
CE1 A:HIS248 3.3 14.5 1.0
ND1 A:HIS248 3.4 13.3 1.0
CB A:ARG293 3.5 12.5 1.0
CG A:ARG293 3.5 13.0 1.0
CD A:ARG293 3.6 13.9 1.0
CZ A:ARG243 3.7 15.5 1.0
CA A:ARG293 3.8 12.5 1.0
O A:ARG293 3.8 14.9 1.0
OH A:TYR257 3.9 14.8 1.0
CH2 A:TRP304 4.1 17.4 1.0
C A:ARG293 4.1 12.9 1.0
CZ2 A:TRP304 4.2 17.3 1.0
CZ A:ARG293 4.2 15.5 1.0
NE A:ARG293 4.4 16.1 1.0
NE2 A:HIS248 4.4 13.9 1.0
CG A:HIS248 4.6 13.2 1.0
O A:HOH803 4.7 19.0 1.0
CZ3 A:TRP304 4.8 16.3 1.0
CE2 A:TRP304 4.9 15.4 1.0
CZ A:TYR257 4.9 12.1 1.0

Chlorine binding site 2 out of 4 in 3ecj

Go back to Chlorine Binding Sites List in 3ecj
Chlorine binding site 2 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:18.8
occ:1.00
 O B:HOH1014 3.1 29.6 1.0
NH1 B:ARG243 3.2 14.6 1.0
NH2 B:ARG243 3.2 14.1 1.0
NH1 B:ARG293 3.2 14.1 1.0
CE1 B:HIS248 3.3 14.9 1.0
ND1 B:HIS248 3.4 13.2 1.0
CB B:ARG293 3.5 12.2 1.0
CG B:ARG293 3.5 13.3 1.0
CD B:ARG293 3.6 12.7 1.0
CZ B:ARG243 3.7 13.2 1.0
O B:ARG293 3.8 12.9 1.0
CA B:ARG293 3.8 11.6 1.0
OH B:TYR257 3.9 13.7 1.0
CH2 B:TRP304 4.1 15.8 1.0
C B:ARG293 4.1 11.7 1.0
CZ2 B:TRP304 4.2 15.3 1.0
CZ B:ARG293 4.3 16.1 1.0
NE B:ARG293 4.4 13.8 1.0
NE2 B:HIS248 4.4 12.4 1.0
CG B:HIS248 4.6 13.2 1.0
O B:HOH1010 4.7 17.9 1.0
CZ3 B:TRP304 4.7 15.5 1.0
CE2 B:TRP304 4.9 13.1 1.0
CZ B:TYR257 4.9 13.2 1.0
NE B:ARG243 5.0 14.7 1.0

Chlorine binding site 3 out of 4 in 3ecj

Go back to Chlorine Binding Sites List in 3ecj
Chlorine binding site 3 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl501

b:20.3
occ:1.00
 O C:HOH809 3.2 29.9 1.0
CE1 C:HIS248 3.2 15.4 1.0
ND1 C:HIS248 3.3 15.5 1.0
NH1 C:ARG293 3.3 16.0 1.0
NH1 C:ARG243 3.3 16.1 1.0
NH2 C:ARG243 3.4 14.1 1.0
CB C:ARG293 3.5 15.8 1.0
CG C:ARG293 3.5 15.3 1.0
CD C:ARG293 3.7 16.4 1.0
O C:ARG293 3.7 15.9 1.0
CA C:ARG293 3.8 15.0 1.0
CZ C:ARG243 3.8 14.7 1.0
OH C:TYR257 3.9 14.6 1.0
C C:ARG293 4.1 15.4 1.0
CH2 C:TRP304 4.1 17.4 1.0
CZ2 C:TRP304 4.2 16.8 1.0
CZ C:ARG293 4.3 16.4 1.0
NE2 C:HIS248 4.4 12.6 1.0
NE C:ARG293 4.5 14.9 1.0
CG C:HIS248 4.6 14.3 1.0
O C:HOH806 4.7 14.6 1.0
CZ3 C:TRP304 4.7 17.7 1.0
CE2 C:TRP304 5.0 14.2 1.0
CZ C:TYR257 5.0 11.6 1.0

Chlorine binding site 4 out of 4 in 3ecj

Go back to Chlorine Binding Sites List in 3ecj
Chlorine binding site 4 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl501

b:16.4
occ:1.00
 NH1 D:ARG293 3.1 13.5 1.0
NH1 D:ARG243 3.2 11.4 1.0
NH2 D:ARG243 3.3 11.3 1.0
O D:HOH836 3.3 26.3 1.0
CE1 D:HIS248 3.3 13.9 1.0
ND1 D:HIS248 3.4 12.8 1.0
CG D:ARG293 3.6 12.0 1.0
CB D:ARG293 3.6 12.6 1.0
CD D:ARG293 3.6 12.4 1.0
CZ D:ARG243 3.7 10.8 1.0
O D:ARG293 3.8 14.8 1.0
CA D:ARG293 3.8 12.7 1.0
OH D:TYR257 3.9 11.5 1.0
CH2 D:TRP304 4.1 15.2 1.0
C D:ARG293 4.2 13.3 1.0
CZ D:ARG293 4.2 14.4 1.0
CZ2 D:TRP304 4.2 14.2 1.0
NE D:ARG293 4.3 13.4 1.0
NE2 D:HIS248 4.5 11.5 1.0
CG D:HIS248 4.6 11.8 1.0
O D:HOH833 4.7 11.8 1.0
CZ3 D:TRP304 4.8 14.3 1.0
CE2 D:TRP304 4.9 12.7 1.0
CZ D:TYR257 4.9 8.6 1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Intermediate in the O-O Bond Cleavage Reaction of An Extradiol Dioxygenase. Biochemistry V. 47 11168 2008.
ISSN: ISSN 0006-2960
PubMed: 18826259
DOI: 10.1021/BI801459Q
Page generated: Sat Jul 20 18:47:20 2024

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