Calcium in PDB 5mn1: Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K)

All present enzymatic activity of Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K):
3.4.21.4;

The structure of Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K), PDB code: 5mn1 was solved by J.Schiebel, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.35 / 0.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.692, 58.269, 66.936, 90.00, 90.00, 90.00
R / Rfree (%)	9.8 / 10.9

The binding sites of Calcium atom in the Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K) (pdb code 5mn1). 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 Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K), PDB code: 5mn1:

Calcium binding site 1 out of 1 in the Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cationic Trypsin in Complex with 2-Aminopyridine (Deuterated Sample at 100 K) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:5.5 occ:1.00 OE1 A:GLU70 2.3 6.3 1.0 O A:VAL75 2.3 6.3 1.0 O A:ASN72 2.3 5.8 1.0 OE2 A:GLU80 2.3 6.3 1.0 O A:HOH545 2.3 6.7 1.0 O A:HOH419 2.4 6.1 1.0 H2 A:HOH419 2.7 7.3 1.0 H1 A:HOH419 3.1 7.3 1.0 H2 A:HOH545 3.1 8.1 1.0 CD A:GLU70 3.3 5.6 1.0 HA A:VAL76 3.4 8.0 1.0 CD A:GLU80 3.4 6.5 1.0 C A:VAL75 3.4 6.1 1.0 C A:ASN72 3.5 5.4 1.0 H A:VAL75 3.5 7.1 1.0 H A:GLU77 3.5 8.2 0.4 H A:GLU77 3.5 8.2 0.6 HA A:ILE73 3.6 6.7 1.0 HG3 A:GLU77 3.7 8.3 0.4 CG A:GLU80 3.8 8.4 1.0 OE2 A:GLU70 3.8 6.4 1.0 HG3 A:GLU77 3.8 9.8 0.6 H A:ASP71 3.8 6.7 1.0 HA A:GLU70 3.9 6.5 1.0 CA A:VAL76 4.1 6.6 1.0 N A:GLU77 4.2 6.8 0.6 N A:GLU77 4.2 6.9 0.4 N A:VAL76 4.2 6.5 1.0 N A:VAL75 4.2 5.9 1.0 OE1 A:GLU77 4.2 8.0 0.6 HB3 A:ASN72 4.2 8.2 1.0 CA A:ILE73 4.3 5.6 1.0 OE1 A:GLU77 4.3 6.4 0.4 H A:ASN72 4.3 7.0 1.0 N A:ILE73 4.3 5.7 1.0 N A:ASN72 4.4 5.8 1.0 CA A:VAL75 4.4 6.2 1.0 O A:HOH548 4.5 7.1 1.0 CA A:ASN72 4.5 5.7 1.0 HB3 A:GLU70 4.5 6.4 1.0 CG A:GLU77 4.5 8.2 0.6 OE1 A:GLU80 4.5 7.0 1.0 CG A:GLU77 4.5 7.0 0.4 C A:ILE73 4.5 5.6 1.0 N A:ASP71 4.6 5.6 1.0 H2 A:HOH501 4.6 7.6 1.0 CG A:GLU70 4.6 5.6 1.0 HB A:VAL75 4.6 8.1 1.0 C A:VAL76 4.7 7.1 1.0 CA A:GLU70 4.7 5.4 1.0 CD A:GLU77 4.7 8.6 0.6 CB A:GLU77 4.8 8.0 0.6 CB A:GLU77 4.8 7.0 0.4 CB A:GLU70 4.8 5.4 1.0 O A:HOH685 4.8 11.6 1.0 CB A:ASN72 4.9 6.8 1.0 N A:ASN74 4.9 5.6 1.0 CD A:GLU77 4.9 7.5 0.4 HG22 A:VAL76 4.9 9.6 1.0 H A:ASN74 4.9 6.8 0.1 H A:ASN74 4.9 6.8 0.9 O A:ILE73 5.0 6.4 1.0 C A:ASP71 5.0 5.7 1.0 HG2 A:GLU70 5.0 6.7 1.0 H A:VAL76 5.0 7.8 1.0

J.Schiebel, R.Gaspari, A.Sandner, K.Ngo, H.D.Gerber, A.Cavalli, A.Ostermann, A.Heine, G.Klebe. Charges Shift Protonation: Neutron Diffraction Reveals That Aniline and 2-Aminopyridine Become Protonated Upon Binding to Trypsin. Angew. Chem. Int. Ed. Engl. V. 56 4887 2017.
ISSN: ESSN 1521-3773
PubMed: 28371253
DOI: 10.1002/ANIE.201701038