Calcium in PDB 4hte: Crystal Structure of the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus

The structure of Crystal Structure of the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus, PDB code: 4hte was solved by L.Betts, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.81 / 3.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.284, 75.284, 179.849, 90.00, 90.00, 90.00
R / Rfree (%)	26.7 / 29.2

The binding sites of Calcium atom in the Crystal Structure of the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus (pdb code 4hte). 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 the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus, PDB code: 4hte:

Calcium binding site 1 out of 1 in the Crystal Structure of the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus


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 the C-Terminal Domain of Nicking Enzyme From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:62.3 occ:0.89 HZ2 A:LYS516 3.7 73.8 1.0 OD1 A:ASP561 3.7 60.5 1.0 OD2 A:ASP561 3.7 66.0 1.0 OD1 A:ASP569 3.7 58.4 1.0 O A:THR497 3.8 64.1 1.0 CG A:ASP561 3.9 61.8 1.0 O A:ASP561 3.9 58.9 1.0 HZ1 A:LYS516 4.0 73.8 1.0 OD2 A:ASP569 4.0 54.4 1.0 NZ A:LYS516 4.1 61.5 1.0 HZ3 A:LYS516 4.2 73.8 1.0 CG A:ASP569 4.3 54.6 1.0 HA A:TYR498 4.3 75.7 1.0 HB2 A:ASP563 4.4 60.2 1.0 C A:ASP561 4.9 53.8 1.0 C A:THR497 4.9 64.0 1.0

J.S.Edwards, L.Betts, M.L.Frazier, R.M.Pollet, S.M.Kwong, W.G.Walton, W.K.Ballentine, J.J.Huang, S.Habibi, M.Del Campo, J.L.Meier, P.B.Dervan, N.Firth, M.R.Redinbo. Molecular Basis of Antibiotic Multiresistance Transfer in Staphylococcus Aureus. Proc.Natl.Acad.Sci.Usa V. 110 2804 2013.
ISSN: ISSN 0027-8424
PubMed: 23359708
DOI: 10.1073/PNAS.1219701110