Calcium in PDB 8emr: Cryo-Em Structure of Human Liver Glucosidase II

All present enzymatic activity of Cryo-Em Structure of Human Liver Glucosidase II:
3.2.1.207;

The binding sites of Calcium atom in the Cryo-Em Structure of Human Liver Glucosidase II (pdb code 8emr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cryo-Em Structure of Human Liver Glucosidase II, PDB code: 8emr:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Cryo-Em Structure of Human Liver Glucosidase II


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of Human Liver Glucosidase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca601 b:119.9 occ:1.00 O B:ARG91 2.3 114.0 1.0 O B:VAL96 2.3 111.4 1.0 OD2 B:ASP104 2.3 125.6 1.0 OE2 B:GLU105 2.4 122.9 1.0 OD2 B:ASP98 2.4 129.3 1.0 OD1 B:ASP94 2.4 116.2 1.0 CG B:ASP104 3.0 125.7 1.0 CG B:ASP94 3.3 112.2 1.0 CB B:ASP104 3.3 121.6 1.0 OD2 B:ASP94 3.5 112.5 1.0 C B:ARG91 3.5 112.9 1.0 CG B:ASP98 3.5 128.0 1.0 C B:VAL96 3.5 108.5 1.0 CD B:GLU105 3.6 119.7 1.0 OD1 B:ASP104 3.9 128.5 1.0 N B:ASP98 3.9 129.0 1.0 CB B:ASP98 4.1 121.3 1.0 CA B:ARG91 4.2 111.0 1.0 CA B:CYS97 4.3 118.6 1.0 CB B:ARG91 4.3 110.1 1.0 N B:CYS97 4.3 116.3 1.0 C B:CYS97 4.3 123.5 1.0 OE1 B:GLU105 4.4 118.9 1.0 N B:VAL96 4.4 110.7 1.0 N B:VAL92 4.5 106.8 1.0 N B:ASP94 4.5 116.2 1.0 OD1 B:ASP98 4.5 129.2 1.0 CA B:VAL96 4.5 111.0 1.0 CG B:GLU105 4.6 122.6 1.0 CA B:ASP104 4.6 117.5 1.0 CA B:VAL92 4.6 101.7 1.0 N B:ASN93 4.6 113.4 1.0 CB B:ASP94 4.7 112.8 1.0 CA B:ASP98 4.7 123.6 1.0 C B:ASP104 4.7 121.8 1.0 C B:VAL92 4.9 104.2 1.0 O B:ASP104 4.9 123.5 1.0

Calcium binding site 2 out of 2 in the Cryo-Em Structure of Human Liver Glucosidase II


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cryo-Em Structure of Human Liver Glucosidase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca602 b:96.6 occ:1.00 OD1 B:ASP53 2.3 106.0 1.0 O B:GLN50 2.3 104.7 1.0 OD2 B:ASP63 2.3 118.3 1.0 O B:TYR55 2.3 96.1 1.0 OD2 B:ASP57 2.4 118.7 1.0 OE2 B:GLU64 2.4 117.9 1.0 CG B:ASP53 3.3 106.1 1.0 CG B:ASP57 3.4 117.9 1.0 C B:TYR55 3.5 97.0 1.0 CD B:GLU64 3.5 110.7 1.0 C B:GLN50 3.5 107.5 1.0 CG B:ASP63 3.5 118.5 1.0 OD2 B:ASP53 3.6 109.8 1.0 CG B:GLU64 4.1 103.5 1.0 OD1 B:ASP57 4.1 115.0 1.0 N B:ASP57 4.1 112.8 1.0 N B:TYR55 4.2 101.4 1.0 CB B:ASP63 4.2 118.2 1.0 N B:ASP53 4.2 103.0 1.0 CA B:TYR55 4.2 97.2 1.0 CB B:ASP57 4.3 112.7 1.0 NH2 A:ARG929 4.3 85.3 1.0 O B:ASP63 4.3 120.0 1.0 CB B:GLN50 4.3 108.8 1.0 CB B:TYR55 4.4 99.9 1.0 N B:ASN52 4.4 107.7 1.0 CA B:GLN50 4.4 107.8 1.0 N B:VAL51 4.4 115.8 1.0 CA B:VAL51 4.5 114.9 1.0 N B:CYS56 4.5 103.0 1.0 OE1 B:GLU64 4.5 113.2 1.0 OD1 B:ASP63 4.5 120.5 1.0 CB B:ASP53 4.5 104.5 1.0 C B:VAL51 4.7 118.2 1.0 CA B:CYS56 4.7 107.3 1.0 C B:ASP63 4.8 119.4 1.0 CA B:ASP53 4.8 104.2 1.0 CA B:ASP57 4.8 110.3 1.0 C B:CYS56 4.9 107.8 1.0 CD1 B:ILE46 5.0 117.0 1.0

C.Su, M.Lyu, Z.Zhang, E.W.Yu. Cryo-Em Structure of Human Liver Glucosidase II To Be Published.