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Chlorine in PDB 4hnv: Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase
Enzymatic activity of Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase
All present enzymatic activity of Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase:
6.4.1.1;
6.4.1.1;
Protein crystallography data
The structure of Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase, PDB code: 4hnv
was solved by
L.P.C.Yu,
L.Tong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 30.00 / 2.80 |
| Space group | P 1 21 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 96.434, 256.742, 127.045, 90.00, 109.33, 90.00 |
| R / Rfree (%) | 19.4 / 26.2 |
Other elements in 4hnv:
The structure of Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase also contains other interesting chemical elements:
| Manganese | (Mn) | 4 atoms |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase
(pdb code 4hnv). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase, PDB code: 4hnv:
In total only one binding site of Chlorine was determined in the Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase, PDB code: 4hnv:
Chlorine binding site 1 out of 1 in 4hnv
Go back to
Chlorine Binding Sites List in 4hnv
Chlorine binding site 1 out
of 1 in the Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Crystal Structure of R54E Mutant of S. Aureus Pyruvate Carboxylase within 5.0Å range:
|
Reference:
L.P.Yu,
C.Y.Chou,
P.H.Choi,
L.Tong.
Characterizing the Importance of the Biotin Carboxylase Domain Dimer For Staphylococcus Aureus Pyruvate Carboxylase Catalysis. Biochemistry V. 52 488 2013.
ISSN: ISSN 0006-2960
PubMed: 23286247
DOI: 10.1021/BI301294D
Page generated: Fri Jul 11 16:26:27 2025
ISSN: ISSN 0006-2960
PubMed: 23286247
DOI: 10.1021/BI301294D
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