Calcium in PDB 7n3y: Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna

The structure of Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna, PDB code: 7n3y was solved by J.L.Wojtaszek, J.Krahn, B.D.Wallace, R.S.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.97 / 2.73
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.408, 101.473, 144.973, 90, 90.14, 90
R / Rfree (%)	20 / 22.8

The binding sites of Calcium atom in the Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna (pdb code 7n3y). 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 Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna, PDB code: 7n3y:

Calcium binding site 1 out of 1 in the Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Saccharomyces Cerevisiae APN2 Catalytic Domain E59Q/D222N Mutant in Complex with Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:108.8 occ:1.00 O A:HOH652 3.0 72.6 1.0 O A:HOH605 3.4 60.8 1.0 OD1 A:ASP53 3.7 58.1 1.0 NZ A:LYS12 3.9 53.6 1.0 O A:HOH644 3.9 64.9 1.0 O A:ARG51 4.1 54.0 1.0 NE A:ARG97 4.3 42.8 1.0 CD A:LYS12 4.4 55.6 1.0 C A:ARG51 4.4 48.8 1.0 CZ A:ARG97 4.4 52.5 1.0 NH2 A:ARG97 4.5 54.9 1.0 CA A:ARG51 4.5 45.9 1.0 CE A:LYS12 4.6 52.5 1.0 CG A:ASP53 4.6 47.1 1.0 CB A:ARG51 4.7 45.1 1.0 OD2 A:ASP53 4.8 52.6 1.0 CD A:ARG97 4.9 43.2 1.0

J.S.Williams, J.L.Wojtaszek, D.C.Appel, J.Krahn, B.D.Wallace, E.Walsh, T.A.Kunkel, R.S.Williams. Molecular Basis For Processing of Topoisomerase 1-Triggered Dna Damage By APN2/APE2. Cell Rep V. 41 11448 2022.
ISSN: ESSN 2211-1247
PubMed: 36198268
DOI: 10.1016/J.CELREP.2022.111448