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

The structure of IFIT1 Monomeric Mutant (L457E/L464E) with Gppp-Aaaa, PDB code: 5udj 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)	40.30 / 1.69
Space group	P 42 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.536, 112.536, 93.470, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 18.1

The binding sites of Calcium atom in the IFIT1 Monomeric Mutant (L457E/L464E) with Gppp-Aaaa (pdb code 5udj). 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 Gppp-Aaaa, PDB code: 5udj:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the IFIT1 Monomeric Mutant (L457E/L464E) with Gppp-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 Gppp-Aaaa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:15.8 occ:0.47 O A:HOH788 2.3 27.9 1.0 O A:HOH842 2.4 41.5 1.0 OD2 A:ASP47 2.4 31.2 1.0 OD1 A:ASP47 2.5 32.7 1.0 CG A:ASP47 2.8 30.1 1.0 H A:SER249 3.9 26.4 1.0 HA A:SER248 4.3 30.1 1.0 CB A:ASP47 4.3 24.8 1.0 HA A:PHE45 4.4 17.6 1.0 O A:PHE45 4.6 15.4 1.0 O A:HOH664 4.6 36.4 1.0 O A:HOH760 4.7 22.3 1.0 HB2 A:ASP47 4.7 29.7 1.0 HB3 A:ASP47 4.8 29.7 1.0 N A:SER249 4.8 22.0 1.0 O A:GLU44 4.8 14.7 1.0 HA A:ASP47 4.9 24.8 1.0 C A:PHE45 5.0 14.2 1.0

Calcium binding site 2 out of 2 in the IFIT1 Monomeric Mutant (L457E/L464E) with Gppp-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 Gppp-Aaaa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca503 b:45.7 occ:1.00 OE1 A:GLU77 2.5 39.9 1.0 OE2 A:GLU77 2.7 47.1 1.0 O A:HOH900 2.7 42.1 1.0 CD A:GLU77 2.9 41.2 1.0 O A:HOH708 4.3 20.5 1.0 HE1 A:HIS55 4.4 22.9 1.0 CG A:GLU77 4.5 32.0 1.0 HB2 A:GLU77 4.8 30.9 1.0 HG3 A:GLU77 4.8 38.4 1.0 HG2 A:GLU77 4.9 38.4 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