Calcium in PDB 5hr4: Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities

The structure of Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities, PDB code: 5hr4 was solved by S.J.Callahan, Y.A.Luyten, Y.K.Gupta, G.G.Wilson, R.J.Roberts, R.D.Morgan, A.K.Aggarwal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.05 / 2.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	61.877, 95.292, 161.969, 72.84, 89.15, 71.62
R / Rfree (%)	21.5 / 24.2

The binding sites of Calcium atom in the Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities (pdb code 5hr4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities, PDB code: 5hr4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1001 b:39.1 occ:1.00 O C:LEU285 2.2 42.0 1.0 O C:CYS283 2.3 41.6 1.0 OE1 C:GLN158 2.4 44.6 1.0 O C:HOH1119 2.4 36.8 1.0 OD1 C:ASP201 2.4 35.3 1.0 OD2 C:ASP201 2.4 32.0 1.0 CG C:ASP201 2.7 34.1 1.0 C C:LEU285 3.4 41.1 1.0 CD C:GLN158 3.4 45.4 1.0 C C:CYS283 3.5 42.6 1.0 NE2 C:GLN158 3.8 40.0 1.0 C C:SER284 4.1 43.9 1.0 N C:LEU285 4.1 39.4 1.0 CB C:ASP201 4.2 32.8 1.0 N C:ASP286 4.2 39.4 1.0 CA C:ASP286 4.3 39.2 1.0 CA C:CYS283 4.4 46.1 1.0 O C:SER284 4.4 48.8 1.0 CA C:LEU285 4.4 36.5 1.0 CA C:SER284 4.4 46.8 1.0 N C:SER284 4.4 41.8 1.0 OE2 C:GLU200 4.5 48.1 1.0 CD1 C:TRP287 4.5 30.2 1.0 CG C:GLU200 4.6 39.8 1.0 OE1 C:GLN211 4.7 49.0 1.0 CG C:GLN158 4.7 45.3 1.0 CD C:GLU200 4.7 48.3 1.0 O C:LEU282 4.8 37.6 1.0 N C:TRP287 4.9 35.9 1.0 CB C:GLN158 4.9 39.8 1.0 CA C:ASP201 5.0 37.0 1.0 O C:LEU197 5.0 29.4 1.0

Calcium binding site 2 out of 2 in the Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering of New Specificities within 5.0Å range: probe atom residue distance (Å) B Occ J:Ca1001 b:37.0 occ:1.00 O J:HOH1122 2.2 28.3 1.0 O J:LEU285 2.2 37.8 1.0 O J:CYS283 2.3 36.9 1.0 OD2 J:ASP201 2.3 38.1 1.0 O J:HOH1125 2.4 37.4 1.0 OD1 J:ASP201 2.4 40.5 1.0 OE1 J:GLN158 2.4 41.5 1.0 CG J:ASP201 2.7 40.0 1.0 CD J:GLN158 3.2 39.4 1.0 C J:LEU285 3.4 41.9 1.0 NE2 J:GLN158 3.4 42.8 1.0 C J:CYS283 3.5 35.4 1.0 N J:LEU285 3.9 39.4 1.0 CB J:ASP201 4.2 33.2 1.0 OE2 J:GLU200 4.2 44.1 1.0 C J:SER284 4.2 40.2 1.0 CG J:GLU200 4.2 33.9 1.0 CA J:LEU285 4.3 36.2 1.0 N J:ASP286 4.3 42.8 1.0 CD1 J:TRP287 4.4 33.8 1.0 CA J:CYS283 4.4 36.1 1.0 CA J:ASP286 4.4 40.3 1.0 CD J:GLU200 4.4 43.0 1.0 N J:SER284 4.5 36.5 1.0 CA J:SER284 4.5 38.6 1.0 CG J:GLN158 4.6 39.5 1.0 OE1 J:GLN211 4.7 42.2 1.0 O J:LEU197 4.7 38.3 1.0 O J:SER284 4.7 43.5 1.0 OG J:SER208 4.8 37.8 1.0 O J:LEU282 4.9 39.9 1.0 CB J:GLN158 4.9 46.9 1.0 CA J:ASP201 4.9 36.0 1.0 NE1 J:TRP287 4.9 35.3 1.0

S.J.Callahan, Y.A.Luyten, Y.K.Gupta, G.G.Wilson, R.J.Roberts, R.D.Morgan, A.K.Aggarwal. Structure of Type Iil Restriction-Modification Enzyme Mmei in Complex with Dna Has Implications For Engineering New Specificities. Plos Biol. V. 14 02442 2016.
ISSN: ESSN 1545-7885
PubMed: 27082731
DOI: 10.1371/JOURNAL.PBIO.1002442