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Manganese in PDB 1rx8: Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose

Enzymatic activity of Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose

All present enzymatic activity of Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose:
1.5.1.3;

Protein crystallography data

The structure of Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose, PDB code: 1rx8 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 / 2.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.430, 45.035, 99.259, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose (pdb code 1rx8). 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 Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose, PDB code: 1rx8:

Manganese binding site 1 out of 1 in 1rx8

Go back to Manganese Binding Sites List in 1rx8
Manganese binding site 1 out of 1 in the Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Dihydrofolate Reductase Complexed with Folate and 2'- Monophosphoadenosine 5'-Diphosphoribose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn300

b:67.1
occ:1.00
 O A:HOH383 1.9 42.5 1.0
O A:HOH424 2.1 78.6 1.0
O A:HOH425 2.1 48.5 1.0
O A:ARG159 2.5 37.2 1.0
C A:ARG159 3.7 33.9 1.0
CA A:ARG159 4.3 34.2 1.0
OXT A:ARG159 4.7 31.4 1.0
O A:ARG158 4.7 32.2 1.0
CB A:ARG159 5.0 35.5 1.0

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 12:21:32 2024

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