Calcium in PDB 1bty: Crystal Structure of Beta-Trypsin in Complex with Benzamidine

All present enzymatic activity of Crystal Structure of Beta-Trypsin in Complex with Benzamidine:
3.4.21.4;

The structure of Crystal Structure of Beta-Trypsin in Complex with Benzamidine, PDB code: 1bty was solved by R.M.Stroud, B.A.Katz, J.Finer-Moore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.840, 58.610, 67.470, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / n/a

The binding sites of Calcium atom in the Crystal Structure of Beta-Trypsin in Complex with Benzamidine (pdb code 1bty). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Beta-Trypsin in Complex with Benzamidine, PDB code: 1bty:

Calcium binding site 1 out of 1 in the Crystal Structure of Beta-Trypsin in Complex with Benzamidine


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 Beta-Trypsin in Complex with Benzamidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca247 b:24.1 occ:1.00 O A:VAL75 2.1 11.2 1.0 O A:ASN72 2.2 8.9 1.0 O A:HOH250 2.3 10.2 1.0 O A:HOH260 2.3 18.5 1.0 OE1 A:GLU70 2.4 10.5 1.0 OE2 A:GLU80 2.4 12.8 1.0 H2 A:HOH250 3.0 10.8 1.0 H1 A:HOH260 3.0 19.8 1.0 H1 A:HOH250 3.1 11.3 1.0 H2 A:HOH260 3.1 19.0 1.0 HA A:VAL76 3.2 14.0 1.0 C A:VAL75 3.2 12.5 1.0 CD A:GLU70 3.3 12.7 1.0 C A:ASN72 3.4 11.9 1.0 H A:VAL75 3.4 12.1 1.0 H A:GLU77 3.4 14.8 1.0 HG3 A:GLU77 3.5 16.0 1.0 HA A:ILE73 3.5 11.3 1.0 CD A:GLU80 3.5 13.8 1.0 HG2 A:GLU80 3.6 12.5 1.0 H A:ASP71 3.6 11.6 1.0 OE2 A:GLU70 3.7 11.5 1.0 HB3 A:ASN72 3.9 13.6 1.0 CA A:VAL76 3.9 13.6 1.0 N A:VAL76 4.0 13.3 1.0 N A:VAL75 4.0 11.1 1.0 CG A:GLU80 4.0 12.8 1.0 HA A:GLU70 4.0 10.7 1.0 H A:ASN72 4.0 13.4 1.0 N A:GLU77 4.0 14.1 1.0 HG3 A:GLU80 4.1 12.6 1.0 CA A:VAL75 4.2 11.7 1.0 CA A:ILE73 4.2 11.6 1.0 OE1 A:GLU77 4.2 15.5 1.0 N A:ILE73 4.2 11.7 1.0 N A:ASN72 4.2 12.5 1.0 CA A:ASN72 4.3 12.0 1.0 HB A:VAL75 4.3 13.1 1.0 CG A:GLU77 4.3 16.4 1.0 O A:HOH267 4.4 15.2 1.0 C A:ILE73 4.4 10.6 1.0 C A:VAL76 4.4 16.1 1.0 HB2 A:GLU77 4.4 15.7 1.0 HB3 A:GLU70 4.5 12.0 1.0 OE1 A:GLU80 4.5 12.0 1.0 CB A:ASN72 4.6 12.9 1.0 O A:HOH297 4.6 22.7 1.0 N A:ASP71 4.6 10.8 1.0 N A:ASN74 4.7 9.0 1.0 H A:ASN74 4.7 9.9 1.0 CG A:GLU70 4.7 12.0 1.0 CD A:GLU77 4.7 16.7 1.0 CB A:GLU77 4.8 15.5 1.0 CB A:VAL75 4.8 13.4 1.0 O A:ILE73 4.8 11.7 1.0 HG23 A:VAL76 4.8 15.2 1.0 CA A:GLU70 4.9 11.5 1.0 CB A:GLU70 4.9 12.4 1.0 H A:VAL76 4.9 13.9 1.0 H1 A:HOH267 4.9 15.6 1.0 HZ A:PHE82 5.0 17.4 1.0 C A:ASP71 5.0 12.4 1.0

B.A.Katz, J.Finer-Moore, R.Mortezaei, D.H.Rich, R.M.Stroud. Episelection: Novel Ki Approximately Nanomolar Inhibitors of Serine Proteases Selected By Binding or Chemistry on An Enzyme Surface. Biochemistry V. 34 8264 1995.
ISSN: ISSN 0006-2960
PubMed: 7599119
DOI: 10.1021/BI00026A008