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Chlorine in PDB 4ghc: Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution

Enzymatic activity of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution

All present enzymatic activity of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution, PDB code: 4ghc 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) 22.47 / 1.55
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.356, 151.736, 96.335, 90.00, 90.00, 90.00
R / Rfree (%) 11.7 / 14.8

Other elements in 4ghc:

The structure of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution (pdb code 4ghc). 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution, PDB code: 4ghc:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 4ghc

Go back to Chlorine Binding Sites List in 4ghc
Chlorine binding site 1 out of 4 in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:11.6
occ:1.00
 NH1 A:ARG243 3.2 10.4 1.0
NH1 A:ARG293 3.2 9.0 1.0
O A:HOH770 3.2 21.7 1.0
CE1 A:HIS248 3.3 9.2 1.0
NH2 A:ARG243 3.3 9.4 1.0
ND1 A:HIS248 3.4 9.3 1.0
CB A:ARG293 3.5 8.1 1.0
CG A:ARG293 3.6 8.3 1.0
CD A:ARG293 3.6 8.7 1.0
CZ A:ARG243 3.7 9.8 1.0
O A:ARG293 3.8 8.5 1.0
CA A:ARG293 3.9 7.9 1.0
CZ2 A:TRP304 4.0 10.8 1.0
CH2 A:TRP304 4.1 11.6 1.0
C A:ARG293 4.2 7.7 1.0
CZ A:ARG293 4.2 8.6 1.0
NE A:ARG293 4.4 8.6 1.0
NE2 A:HIS248 4.5 9.2 1.0
O A:HOH867 4.5 13.9 1.0
CE2 A:TRP304 4.6 10.3 1.0
CG A:HIS248 4.6 8.4 1.0
CZ3 A:TRP304 4.7 11.1 1.0
CE2 A:PHE257 4.8 8.9 1.0
CZ A:PHE257 4.8 9.0 1.0

Chlorine binding site 2 out of 4 in 4ghc

Go back to Chlorine Binding Sites List in 4ghc
Chlorine binding site 2 out of 4 in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl403

b:10.3
occ:1.00
 NH1 B:ARG243 3.1 9.5 1.0
O B:HOH817 3.2 20.2 1.0
NH1 B:ARG293 3.2 9.4 1.0
NH2 B:ARG243 3.3 9.3 1.0
CE1 B:HIS248 3.3 8.2 1.0
ND1 B:HIS248 3.4 8.3 1.0
CB B:ARG293 3.5 8.7 1.0
CG B:ARG293 3.6 8.8 1.0
CD B:ARG293 3.6 9.0 1.0
CZ B:ARG243 3.7 8.9 1.0
O B:ARG293 3.8 8.8 1.0
CA B:ARG293 3.9 8.2 1.0
CZ2 B:TRP304 4.1 10.2 1.0
CH2 B:TRP304 4.1 10.7 1.0
C B:ARG293 4.2 8.2 1.0
CZ B:ARG293 4.2 9.2 1.0
NE B:ARG293 4.4 8.9 1.0
NE2 B:HIS248 4.5 8.2 1.0
O B:HOH906 4.5 11.6 1.0
CE2 B:TRP304 4.6 9.1 1.0
CG B:HIS248 4.7 7.8 1.0
CZ3 B:TRP304 4.7 11.2 1.0
CE2 B:PHE257 4.8 8.1 1.0
CZ B:PHE257 4.8 8.3 1.0
NE B:ARG243 5.0 8.6 1.0

Chlorine binding site 3 out of 4 in 4ghc

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Chlorine binding site 3 out of 4 in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl402

b:12.2
occ:1.00
 NH1 C:ARG243 3.2 11.3 1.0
NH1 C:ARG293 3.2 11.3 1.0
CE1 C:HIS248 3.3 10.4 1.0
O C:HOH878 3.3 27.5 1.0
NH2 C:ARG243 3.3 10.6 1.0
ND1 C:HIS248 3.4 9.5 1.0
CB C:ARG293 3.6 10.1 1.0
CG C:ARG293 3.7 10.8 1.0
CD C:ARG293 3.7 10.7 1.0
CZ C:ARG243 3.7 10.8 1.0
O C:ARG293 3.9 10.7 1.0
CA C:ARG293 4.0 10.1 1.0
CZ2 C:TRP304 4.0 12.5 1.0
CH2 C:TRP304 4.1 13.1 1.0
CZ C:ARG293 4.2 10.8 1.0
C C:ARG293 4.3 9.9 1.0
NE C:ARG293 4.4 10.3 1.0
NE2 C:HIS248 4.4 9.7 1.0
O C:HOH831 4.5 13.4 1.0
CG C:HIS248 4.6 9.4 1.0
CE2 C:TRP304 4.7 11.7 1.0
CZ3 C:TRP304 4.7 13.6 1.0
CE2 C:PHE257 4.8 8.4 1.0
CZ C:PHE257 4.8 8.7 1.0

Chlorine binding site 4 out of 4 in 4ghc

Go back to Chlorine Binding Sites List in 4ghc
Chlorine binding site 4 out of 4 in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 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 Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.55 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl402

b:11.1
occ:1.00
 NH1 D:ARG243 3.2 10.2 1.0
O D:HOH740 3.2 21.6 1.0
NH1 D:ARG293 3.3 9.3 1.0
CE1 D:HIS248 3.3 8.4 1.0
NH2 D:ARG243 3.3 9.7 1.0
ND1 D:HIS248 3.4 8.5 1.0
CB D:ARG293 3.6 8.2 1.0
CG D:ARG293 3.6 8.6 1.0
CD D:ARG293 3.7 8.5 1.0
CZ D:ARG243 3.7 9.7 1.0
O D:ARG293 3.8 8.4 1.0
CA D:ARG293 3.9 8.2 1.0
CZ2 D:TRP304 4.0 11.5 1.0
CH2 D:TRP304 4.0 11.5 1.0
C D:ARG293 4.2 8.3 1.0
CZ D:ARG293 4.3 9.2 1.0
NE D:ARG293 4.4 8.7 1.0
NE2 D:HIS248 4.4 8.3 1.0
O D:HOH823 4.5 13.2 1.0
CG D:HIS248 4.6 8.0 1.0
CE2 D:TRP304 4.6 10.4 1.0
CZ3 D:TRP304 4.7 11.8 1.0
CE2 D:PHE257 4.8 9.1 1.0
CZ D:PHE257 4.8 9.0 1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Structural Basis For the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen Activation. Biochemistry V. 51 8755 2012.
ISSN: ISSN 0006-2960
PubMed: 23066739
DOI: 10.1021/BI301115C
Page generated: Fri Jul 11 15:40:09 2025

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