Calcium in PDB 1st3: The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution

All present enzymatic activity of The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution:
3.4.21.62;

The structure of The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution, PDB code: 1st3 was solved by D.W.Goddette, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.60 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.093, 61.490, 75.610, 90.00, 90.00, 90.00
R / Rfree (%)	19 / n/a

The binding sites of Calcium atom in the The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution (pdb code 1st3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution, PDB code: 1st3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca270 b:5.7 occ:1.00 O A:LEU73 2.2 5.3 1.0 O A:ILE77 2.3 7.0 1.0 OE1 A:GLN2 2.3 6.5 1.0 O A:VAL79 2.3 5.2 1.0 OD1 A:ASN75 2.3 4.6 1.0 OD2 A:ASP40 2.4 7.0 1.0 OD1 A:ASP40 2.5 5.9 1.0 CG A:ASP40 2.8 5.9 1.0 CD A:GLN2 3.4 6.2 1.0 CG A:ASN75 3.4 5.2 1.0 C A:LEU73 3.5 5.5 1.0 C A:ILE77 3.5 7.0 1.0 C A:VAL79 3.5 7.1 1.0 N A:VAL79 3.7 6.4 1.0 CG A:GLN2 3.8 9.0 1.0 ND2 A:ASN75 3.9 5.3 1.0 N A:ASN75 4.1 4.9 1.0 C A:GLY78 4.1 6.8 1.0 CA A:VAL79 4.2 6.4 1.0 CA A:GLY78 4.3 7.1 1.0 N A:LEU73 4.3 4.2 1.0 CA A:LEU73 4.3 5.4 1.0 N A:GLY78 4.3 6.7 1.0 CB A:ASP40 4.3 4.5 1.0 N A:ILE77 4.4 4.4 1.0 N A:ASN74 4.4 6.3 1.0 CA A:ILE77 4.5 6.4 1.0 NE2 A:GLN2 4.5 8.2 1.0 CG1 A:ILE77 4.6 9.0 1.0 CB A:GLN2 4.6 9.7 1.0 CA A:ASN74 4.6 6.8 1.0 N A:LEU80 4.6 6.8 1.0 CB A:ASN75 4.6 5.9 1.0 CB A:LEU73 4.7 5.3 1.0 CA A:ASN75 4.7 5.6 1.0 O A:ASN75 4.7 6.1 1.0 O A:GLY78 4.7 5.6 1.0 C A:ASN74 4.7 6.5 1.0 C A:ASN75 4.8 6.3 1.0 CA A:LEU80 4.8 6.2 1.0 C A:ALA72 4.8 4.3 1.0

Calcium binding site 2 out of 2 in the The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca271 b:15.4 occ:1.00 O A:HOH316 1.9 42.6 1.0 O A:HOH273 1.9 23.9 1.0 O A:ALA163 2.2 5.5 1.0 O A:ALA168 2.3 6.2 1.0 O A:TYR165 2.3 6.8 1.0 C A:TYR165 3.3 7.1 1.0 C A:ALA163 3.4 5.5 1.0 C A:ALA168 3.4 6.4 1.0 C A:ARG164 3.7 6.5 1.0 O A:ARG164 3.8 7.0 1.0 N A:TYR165 3.8 6.0 1.0 NH2 A:ARG241 3.9 13.1 1.0 N A:ALA168 4.0 6.6 1.0 CA A:ALA168 4.1 6.5 1.0 O A:ALA166 4.1 9.0 1.0 N A:ALA166 4.1 7.3 1.0 O A:GLY189 4.1 10.0 1.0 CA A:ARG164 4.2 6.9 1.0 CA A:ALA166 4.2 8.2 1.0 N A:ARG164 4.2 6.2 1.0 CA A:TYR165 4.2 7.2 1.0 CB A:ALA168 4.2 6.2 1.0 C A:ALA166 4.2 8.8 1.0 O A:HOH318 4.2 53.9 1.0 OD2 A:ASP191 4.3 12.3 1.0 CB A:ALA170 4.3 5.8 1.0 N A:ALA170 4.4 5.8 1.0 CA A:ALA163 4.4 5.5 1.0 N A:MET169 4.4 6.0 1.0 O A:HOH383 4.5 42.8 1.0 CA A:MET169 4.7 6.3 1.0 O A:PRO162 4.7 5.9 1.0 C A:MET169 4.8 7.6 1.0 N A:ASN167 4.9 8.6 1.0 CZ A:ARG241 4.9 14.0 1.0 CA A:ALA170 5.0 5.4 1.0

D.W.Goddette, C.Paech, S.S.Yang, J.R.Mielenz, C.Bystroff, M.E.Wilke, R.J.Fletterick. The Crystal Structure of the Bacillus Lentus Alkaline Protease, Subtilisin Bl, at 1.4 A Resolution. J.Mol.Biol. V. 228 580 1992.
ISSN: ISSN 0022-2836
PubMed: 1453465
DOI: 10.1016/0022-2836(92)90843-9