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Calcium in PDB 4ibr: Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations
Enzymatic activity of Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations
All present enzymatic activity of Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations:
3.5.2.6;
3.5.2.6;
Protein crystallography data
The structure of Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations, PDB code: 4ibr
was solved by
E.Dellus-Gur,
A.Toth-Petroczy,
M.Elias,
D.S.Tawfik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 67.96 / 2.20 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 136.240, 46.600, 39.000, 90.00, 93.87, 90.00 |
| R / Rfree (%) | 19.5 / 24.7 |
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations
(pdb code 4ibr). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations, PDB code: 4ibr:
In total only one binding site of Calcium was determined in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations, PDB code: 4ibr:
Calcium binding site 1 out of 1 in 4ibr
Go back to
Calcium Binding Sites List in 4ibr
Calcium binding site 1 out
of 1 in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying G238S/E104K Mutations within 5.0Å range:
|
Reference:
E.Dellus-Gur,
A.Toth-Petroczy,
M.Elias,
D.S.Tawfik.
What Makes A Protein Fold Amenable to Functional Innovation? Fold Polarity and Stability Trade-Offs. J.Mol.Biol. V. 425 2609 2013.
ISSN: ISSN 0022-2836
PubMed: 23542341
DOI: 10.1016/J.JMB.2013.03.033
Page generated: Sat Dec 12 04:51:37 2020
ISSN: ISSN 0022-2836
PubMed: 23542341
DOI: 10.1016/J.JMB.2013.03.033
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