Calcium in PDB 3oor: I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate

The structure of I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate, PDB code: 3oor was solved by R.Joshi, J.-H.Chen, B.L.Golden, F.S.Gimble, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.72 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	131.701, 50.538, 62.931, 90.00, 108.46, 90.00
R / Rfree (%)	23.5 / 28.4

The binding sites of Calcium atom in the I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate (pdb code 3oor). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate, PDB code: 3oor:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca236 b:42.2 occ:1.00 OP1 C:DA14 2.1 39.4 1.0 OP1 D:DC17 2.4 50.8 1.0 O A:ASP144 2.4 44.7 1.0 OD2 A:ASP44 2.4 42.5 1.0 CG A:ASP44 3.4 41.1 1.0 C A:ASP144 3.5 45.1 1.0 P D:DC17 3.5 49.9 1.0 P C:DA14 3.6 39.6 1.0 OD1 A:ASP44 3.7 41.7 1.0 OP2 D:DC17 3.9 49.5 1.0 NZ A:LYS223 3.9 57.3 1.0 CA A:ASP144 4.0 45.3 1.0 C5' D:DC17 4.1 56.2 1.0 O5' D:DC17 4.2 52.8 1.0 O3' C:DA13 4.2 38.8 1.0 C5' C:DA14 4.3 36.8 1.0 O A:MET143 4.4 48.8 1.0 O5' C:DA14 4.5 37.7 1.0 OP2 C:DA14 4.5 43.1 1.0 NE1 A:TRP62 4.6 41.3 1.0 N A:ASP145 4.6 45.5 1.0 CD1 A:TRP62 4.6 42.4 1.0 C4' C:DA14 4.7 36.1 1.0 O3' D:DT16 4.8 48.9 1.0 CB A:ASP44 4.8 39.7 1.0 C4' D:DC17 4.8 56.8 1.0 CB A:ASP144 4.9 43.9 1.0

Calcium binding site 2 out of 3 in the I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca237 b:0.9 occ:1.00 OP2 C:DC15 2.2 40.0 1.0 OD1 A:ASP145 2.2 43.5 1.0 O A:GLY43 2.3 38.9 1.0 OD1 A:ASP44 2.3 41.7 1.0 OP2 D:DC17 3.0 49.5 1.0 C A:GLY43 3.0 39.2 1.0 CG A:ASP145 3.1 44.1 1.0 OD2 A:ASP145 3.4 44.9 1.0 CG A:ASP44 3.6 41.1 1.0 P C:DC15 3.6 38.9 1.0 N A:ASP44 3.8 39.0 1.0 CA A:GLY43 3.9 40.2 1.0 CA A:ASP44 3.9 38.7 1.0 CB A:ASP44 4.4 39.7 1.0 P D:DC17 4.4 49.9 1.0 O3' C:DA14 4.4 37.1 1.0 CB A:ASP145 4.4 45.3 1.0 OP1 C:DC15 4.5 39.5 1.0 OD2 A:ASP44 4.5 42.5 1.0 O5' C:DC15 4.5 38.8 1.0 O A:ASN163 4.6 41.9 1.0 O A:ASP144 4.6 44.7 1.0 CA A:ASP145 4.7 45.8 1.0 O A:LEU42 4.7 40.6 1.0 C A:ASP144 4.8 45.1 1.0 OP2 D:DT16 4.9 46.4 1.0 N A:ASP145 4.9 45.5 1.0 CB A:ASP144 4.9 43.9 1.0 C5' C:DC15 4.9 40.6 1.0

Calcium binding site 3 out of 3 in the I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of I-Scei Mutant (K86R/G100T)Complexed with C/G+4 Dna Substrate within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca26 b:47.0 occ:1.00 O D:HOH27 2.2 12.8 1.0 OP1 C:DC15 2.2 39.5 1.0 O C:HOH28 2.2 15.8 1.0 OP1 D:DT16 2.2 45.5 1.0 P D:DT16 3.4 46.0 1.0 P C:DC15 3.6 38.9 1.0 O4' D:DA15 3.6 46.2 1.0 OP2 D:DT16 3.7 46.4 1.0 C4' D:DA15 4.0 46.8 1.0 O3' C:DA14 4.1 37.1 1.0 C1' D:DA15 4.4 47.0 1.0 O4' C:DC15 4.4 39.3 1.0 O3' D:DA15 4.5 47.9 1.0 O5' C:DC15 4.5 38.8 1.0 C4' C:DC15 4.6 40.5 1.0 O5' D:DT16 4.6 47.5 1.0 O4' D:DT16 4.6 46.2 1.0 OP2 C:DC15 4.6 40.0 1.0 N3 D:DA15 4.7 45.9 1.0 C4' D:DT16 4.7 46.4 1.0 C3' D:DA15 4.8 48.0 1.0 O2 D:DT14 4.8 47.0 1.0 C5' C:DC15 4.9 40.6 1.0 C5' D:DT16 5.0 47.4 1.0 N3 C:DA14 5.0 35.1 1.0

R.Joshi, K.K.Ho, K.Tenney, J.H.Chen, B.L.Golden, F.S.Gimble. Evolution of I-Scei Homing Endonucleases with Increased Dna Recognition Site Specificity. J.Mol.Biol. V. 405 185 2011.
ISSN: ISSN 0022-2836
PubMed: 21029741
DOI: 10.1016/J.JMB.2010.10.029