Calcium in PDB 3whi: Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E

All present enzymatic activity of Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E:
3.4.21.62;

The structure of Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E, PDB code: 3whi was solved by R.Uehara, C.Angkawidjaja, Y.Koga, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.40 / 2.40
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	135.202, 135.202, 151.606, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 27

The binding sites of Calcium atom in the Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E (pdb code 3whi). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E, PDB code: 3whi:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E


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 Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:30.0 occ:1.00 OE1 A:GLN92 2.1 29.9 1.0 OD1 A:ASP131 2.2 25.9 1.0 O A:LEU165 2.2 28.0 1.0 O A:ILE169 2.3 34.7 1.0 OD1 A:ASN167 2.4 28.0 1.0 O A:VAL171 2.4 31.1 1.0 OD2 A:ASP131 2.6 28.9 1.0 CG A:ASP131 2.7 29.3 1.0 CD A:GLN92 3.3 32.4 1.0 C A:LEU165 3.4 29.0 1.0 CG A:ASN167 3.4 29.9 1.0 C A:ILE169 3.5 34.3 1.0 C A:VAL171 3.5 30.6 1.0 N A:VAL171 3.6 31.8 1.0 ND2 A:ASN167 4.0 26.8 1.0 N A:ASN167 4.1 32.5 1.0 CG A:GLN92 4.1 35.4 1.0 C A:GLY170 4.2 33.9 1.0 CA A:VAL171 4.2 30.6 1.0 CB A:ASP131 4.2 29.8 1.0 NE2 A:GLN92 4.2 30.0 1.0 CA A:LEU165 4.2 28.8 1.0 N A:LEU165 4.3 27.6 1.0 N A:ILE169 4.4 33.7 1.0 N A:ASN166 4.4 31.1 1.0 N A:GLY170 4.4 33.9 1.0 CA A:ILE169 4.4 33.3 1.0 CG1 A:ILE169 4.5 30.1 1.0 CA A:GLY170 4.5 33.1 1.0 CB A:LEU165 4.5 28.3 1.0 CB A:GLN92 4.6 38.8 1.0 CA A:ASN166 4.6 32.4 1.0 N A:LEU172 4.6 29.8 1.0 CB A:ASN167 4.6 31.6 1.0 C A:ALA164 4.7 27.2 1.0 CA A:ASN167 4.7 32.3 1.0 C A:ASN167 4.8 32.7 1.0 C A:ASN166 4.8 33.0 1.0 CA A:LEU172 4.8 30.6 1.0 O A:GLY170 4.9 34.6 1.0 O A:ALA164 4.9 25.7 1.0 O A:ASN167 4.9 33.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Unautoprocessed Form of IS1-Inserted Pro- Subtilisin E within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:29.6 occ:1.00 O B:LEU165 2.2 31.4 1.0 OD1 B:ASN167 2.2 36.4 1.0 O B:VAL171 2.3 26.9 1.0 OE1 B:GLN92 2.3 31.8 1.0 O B:ILE169 2.4 32.2 1.0 OD1 B:ASP131 2.5 25.8 1.0 OD2 B:ASP131 2.5 28.0 1.0 CG B:ASP131 2.9 29.7 1.0 CG B:ASN167 3.3 37.9 1.0 C B:LEU165 3.4 30.8 1.0 CD B:GLN92 3.4 30.5 1.0 C B:VAL171 3.5 26.7 1.0 C B:ILE169 3.6 32.4 1.0 ND2 B:ASN167 3.7 37.9 1.0 N B:VAL171 3.8 27.8 1.0 N B:ASN167 4.0 37.9 1.0 CG B:GLN92 4.0 31.6 1.0 N B:LEU165 4.2 29.1 1.0 CA B:VAL171 4.2 26.2 1.0 C B:GLY170 4.2 29.4 1.0 CA B:LEU165 4.3 29.8 1.0 CB B:ASP131 4.4 28.8 1.0 N B:ASN166 4.4 32.9 1.0 N B:ILE169 4.4 35.3 1.0 CG1 B:ILE169 4.4 34.4 1.0 CA B:GLY170 4.5 29.7 1.0 N B:GLY170 4.5 30.5 1.0 N B:LEU172 4.5 26.7 1.0 CA B:ILE169 4.5 33.8 1.0 CB B:ASN167 4.5 37.6 1.0 CA B:ASN166 4.5 35.7 1.0 CB B:GLN92 4.6 30.7 1.0 NE2 B:GLN92 4.6 23.4 1.0 CA B:ASN167 4.6 38.5 1.0 C B:ASN166 4.7 36.6 1.0 C B:ASN167 4.7 38.3 1.0 C B:ALA164 4.7 28.5 1.0 O B:ASN167 4.7 38.4 1.0 CB B:LEU165 4.7 29.1 1.0 CA B:LEU172 4.8 25.8 1.0 CB B:ALA164 4.9 27.4 1.0 O B:GLY170 4.9 27.8 1.0

R.Uehara, C.Angkawidjaja, Y.Koga, S.Kanaya. Formation of the High-Affinity Calcium Binding Site in Pro-Subtilisin E with the Insertion Sequence IS1 of Pro-Tk-Subtilisin Biochemistry V. 52 9080 2013.
ISSN: ISSN 0006-2960
PubMed: 24279884
DOI: 10.1021/BI401342K