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Calcium in PDB 6ywn: Cuta in Complex with Cmpcpp

Protein crystallography data

The structure of Cuta in Complex with Cmpcpp, PDB code: 6ywn was solved by D.Malik, K.Kobylecki, P.Krawczyk, J.Poznanski, A.Jakielaszek, A.Napiorkowska, A.Dziembowski, R.Tomecki, M.Nowotny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.08 / 1.45
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.220, 93.470, 86.830, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Cuta in Complex with Cmpcpp (pdb code 6ywn). 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 Cuta in Complex with Cmpcpp, PDB code: 6ywn:

Calcium binding site 1 out of 1 in 6ywn

Go back to Calcium Binding Sites List in 6ywn
Calcium binding site 1 out of 1 in the Cuta in Complex with Cmpcpp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cuta in Complex with Cmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca701

b:16.6
occ:1.00
O1G A:2TM702 2.3 19.0 1.0
O1B A:2TM702 2.4 17.4 1.0
O2A A:2TM702 2.4 17.6 1.0
O A:HOH888 2.5 16.8 1.0
O A:HOH825 2.5 21.6 1.0
OD2 A:ASP339 2.5 19.4 1.0
OD2 A:ASP341 2.5 16.4 1.0
CG A:ASP341 3.4 16.6 1.0
H1 A:2TM702 3.5 20.2 1.0
PG A:2TM702 3.5 17.8 1.0
PB A:2TM702 3.5 16.5 1.0
CG A:ASP339 3.5 21.3 1.0
O3B A:2TM702 3.6 17.0 1.0
H A:SER328 3.7 18.4 1.0
PA A:2TM702 3.7 16.3 1.0
OD1 A:ASP341 3.7 20.4 1.0
H2 A:2TM702 3.7 20.2 1.0
OD1 A:ASP339 3.9 28.6 1.0
C5' A:2TM702 4.0 16.9 1.0
O A:HOH1004 4.0 22.8 1.0
HA3 A:GLY327 4.1 16.8 1.0
C1 A:2TM702 4.2 15.3 1.0
O2G A:2TM702 4.3 18.2 1.0
O A:HOH908 4.3 20.7 1.0
O5' A:2TM702 4.3 16.0 1.0
OG A:SER328 4.4 18.7 1.0
O A:HOH872 4.4 16.5 1.0
HG A:SER328 4.5 22.5 1.0
N A:SER328 4.5 15.3 1.0
O A:ASP339 4.6 16.6 1.0
O A:HOH1103 4.6 38.6 1.0
O3G A:2TM702 4.7 19.0 1.0
H17 A:2TM702 4.7 18.4 1.0
H A:ASP339 4.7 19.7 1.0
CB A:ASP341 4.8 15.5 1.0
H A:ASP341 4.8 20.1 1.0
HB2 A:ASP341 4.8 18.6 1.0
C A:ASP339 4.8 15.8 1.0
O2B A:2TM702 4.9 17.2 1.0
CB A:ASP339 4.9 20.9 1.0
HB3 A:SER328 4.9 22.4 1.0
O1A A:2TM702 4.9 17.4 1.0
CA A:GLY327 5.0 14.0 1.0
H18 A:2TM702 5.0 18.4 1.0
HB3 A:SER338 5.0 24.4 1.0

Reference:

D.Malik, K.Kobylecki, P.Krawczyk, J.Poznanski, A.Jakielaszek, A.Napiorkowska, A.Dziembowski, R.Tomecki, M.Nowotny. Structure and Mechanism of Cuta, Rna Nucleotidyl Transferase with An Unusual Preference For Cytosine. Nucleic Acids Res. V. 48 9387 2020.
ISSN: ESSN 1362-4962
PubMed: 32785623
DOI: 10.1093/NAR/GKAA647
Page generated: Wed Jul 9 20:28:06 2025

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