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Manganese in PDB 1rf7: Structure of Dihydrofolate Reductase Complexed with Dihydrofolate
Enzymatic activity of Structure of Dihydrofolate Reductase Complexed with Dihydrofolate
All present enzymatic activity of Structure of Dihydrofolate Reductase Complexed with Dihydrofolate:
1.5.1.3;
1.5.1.3;
Protein crystallography data
The structure of Structure of Dihydrofolate Reductase Complexed with Dihydrofolate, PDB code: 1rf7
was solved by
M.R.Sawaya,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 20.00 / 1.80 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 34.705, 38.917, 108.827, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 17 / n/a |
Other elements in 1rf7:
The structure of Structure of Dihydrofolate Reductase Complexed with Dihydrofolate also contains other interesting chemical elements:
| Chlorine | (Cl) | 1 atom |
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of Dihydrofolate Reductase Complexed with Dihydrofolate
(pdb code 1rf7). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of Dihydrofolate Reductase Complexed with Dihydrofolate, PDB code: 1rf7:
In total only one binding site of Manganese was determined in the Structure of Dihydrofolate Reductase Complexed with Dihydrofolate, PDB code: 1rf7:
Manganese binding site 1 out of 1 in 1rf7
Go back to
Manganese Binding Sites List in 1rf7
Manganese binding site 1 out
of 1 in the Structure of Dihydrofolate Reductase Complexed with Dihydrofolate
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Structure of Dihydrofolate Reductase Complexed with Dihydrofolate within 5.0Å range:
|
Reference:
M.R.Sawaya,
J.Kraut.
Loop and Subdomain Movements in the Mechanism of Escherichia Coli Dihydrofolate Reductase: Crystallographic Evidence. Biochemistry V. 36 586 1997.
ISSN: ISSN 0006-2960
PubMed: 9012674
DOI: 10.1021/BI962337C
Page generated: Sat Oct 5 12:19:47 2024
ISSN: ISSN 0006-2960
PubMed: 9012674
DOI: 10.1021/BI962337C
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