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Calcium in PDB 1dds: Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate

Enzymatic activity of Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate

All present enzymatic activity of Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate:
1.5.1.3;

Protein crystallography data

The structure of Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate, PDB code: 1dds was solved by H.P.Yennawar, G.K.Farber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.20
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 93.181, 93.185, 73.886, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 20

Other elements in 1dds:

The structure of Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate (pdb code 1dds). 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 Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate, PDB code: 1dds:

Calcium binding site 1 out of 1 in 1dds

Go back to Calcium Binding Sites List in 1dds
Calcium binding site 1 out of 1 in the Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed with Methotrexate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca204

b:18.5
occ:1.00
O B:SER135 3.8 11.1 1.0
OE2 B:GLU134 4.4 7.7 1.0
CA B:VAL136 4.8 8.9 1.0
C B:SER135 5.0 9.7 1.0

Reference:

J.Dunbar, H.P.Yennawar, S.Banerjee, J.Luo, G.K.Farber. The Effect of Denaturants on Protein Structure. Protein Sci. V. 6 1727 1997.
ISSN: ISSN 0961-8368
PubMed: 9260285
Page generated: Sat Dec 12 02:52:44 2020

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