Calcium in PDB 5udk: IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa

The structure of IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa, PDB code: 5udk was solved by Y.M.Abbas, S.Martinez-Montero, M.J.Damha, B.Nagar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.25 / 1.65
Space group	P 42 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.432, 112.432, 93.172, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 18.4

The binding sites of Calcium atom in the IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa (pdb code 5udk). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa, PDB code: 5udk:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca505 b:20.9 occ:0.54 O A:HOH858 2.2 36.3 1.0 O A:HOH765 2.3 33.3 1.0 O A:HOH722 2.3 38.8 1.0 OD1 A:ASP47 2.5 38.5 1.0 OD2 A:ASP47 2.5 36.6 1.0 CG A:ASP47 2.8 37.4 1.0 H A:SER249 3.8 32.2 1.0 HA A:SER248 4.2 33.3 0.5 HA A:SER248 4.2 33.4 0.5 HA A:PHE45 4.2 24.8 1.0 O A:HOH847 4.3 43.4 1.0 CB A:ASP47 4.3 32.5 1.0 O A:PHE45 4.4 22.8 1.0 O A:HOH637 4.5 45.5 1.0 N A:SER249 4.7 26.9 1.0 O A:HOH730 4.7 26.2 1.0 HB3 A:ASP47 4.7 39.0 1.0 HB2 A:ASP47 4.8 39.0 1.0 O A:GLU44 4.8 20.7 1.0 HA A:ASP47 4.8 32.8 1.0 C A:PHE45 4.9 21.3 1.0

Calcium binding site 2 out of 2 in the IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of IFIT1 Monomeric Mutant (L457E/L464E) with Ppp-Aaaa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca506 b:32.3 occ:0.60 OE1 A:GLU77 2.3 74.7 1.0 O A:HOH854 2.5 51.3 1.0 O A:HOH912 2.5 49.9 1.0 O A:HOH867 2.5 42.8 1.0 O A:HOH859 2.6 40.0 1.0 OE2 A:GLU77 2.8 81.8 1.0 CD A:GLU77 2.9 71.3 1.0 O A:HOH735 4.2 23.2 1.0 HE1 A:HIS55 4.4 22.7 1.0 CG A:GLU77 4.4 49.6 1.0 HB2 A:GLU77 4.6 37.4 1.0 HG2 A:GLU77 4.8 59.6 1.0 HG3 A:GLU77 4.9 59.6 1.0

Y.M.Abbas, B.T.Laudenbach, S.Martinez-Montero, R.Cencic, M.Habjan, A.Pichlmair, M.J.Damha, J.Pelletier, B.Nagar. Structure of Human IFIT1 with Capped Rna Reveals Adaptable Mrna Binding and Mechanisms For Sensing N1 and N2 Ribose 2'-O Methylations. Proc. Natl. Acad. Sci. V. 114 E2106 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28251928
DOI: 10.1073/PNAS.1612444114