Calcium in PDB 2ge5: Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+

All present enzymatic activity of Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+:
3.1.21.4;

The structure of Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+, PDB code: 2ge5 was solved by D.A.Hiller, J.J.Perona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.101, 67.101, 259.892, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 28.4

The binding sites of Calcium atom in the Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+ (pdb code 2ge5). 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 Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+, PDB code: 2ge5:

Calcium binding site 1 out of 1 in the Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ecorv Restriction Endonuclease C-Terminal Deletion Mutant/Gatatc/CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca283 b:86.7 occ:1.00 O5' C:DA7 2.8 47.9 1.0 OD2 A:ASP90 2.9 51.2 1.0 OD2 A:ASP74 3.0 58.8 1.0 OP1 C:DA7 3.0 51.2 1.0 O A:HOH292 3.0 67.3 1.0 O A:HOH290 3.2 45.5 1.0 OD1 A:ASP74 3.2 60.2 1.0 OD1 A:ASP90 3.3 51.0 1.0 CG A:ASP90 3.4 49.8 1.0 CG A:ASP74 3.5 57.6 1.0 P C:DA7 3.5 47.9 1.0 O A:ILE91 3.8 40.8 1.0 C5' C:DA7 3.9 46.6 1.0 C4' C:DA7 4.2 44.6 1.0 O3' C:DT6 4.4 47.7 1.0 NZ A:LYS92 4.4 41.9 1.0 N A:ILE91 4.4 43.1 1.0 C3' C:DA7 4.5 45.4 1.0 C A:ILE91 4.7 40.1 1.0 CB A:ASP90 4.7 48.5 1.0 OP2 C:DA7 4.7 47.0 1.0 O3' C:DA7 4.8 46.8 1.0 CE A:LYS92 4.9 45.8 1.0 CB A:ASP74 5.0 56.0 1.0

D.A.Hiller, J.J.Perona. Positively Charged C-Terminal Subdomains of Ecorv Endonuclease: Contributions to Dna Binding, Bending, and Cleavage. Biochemistry V. 45 11453 2006.
ISSN: ISSN 0006-2960
PubMed: 16981705
DOI: 10.1021/BI0606400