Calcium in PDB 5mon: Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine

All present enzymatic activity of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine:
3.4.21.4;

The structure of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine, PDB code: 5mon was solved by J.Schiebel, T.E.Schrader, A.Ostermann, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 0.94
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.989, 58.537, 67.618, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 18.1

The binding sites of Calcium atom in the Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine (pdb code 5mon). 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 Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine, PDB code: 5mon:

Calcium binding site 1 out of 1 in the Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with 2- Aminopyridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:15.7 occ:1.00 OE1 A:GLU70 2.3 17.3 1.0 O A:VAL75 2.3 17.1 1.0 O A:ASN72 2.3 16.2 1.0 OE2 A:GLU80 2.3 17.2 1.0 O A:DOD463 2.4 18.8 1.0 O A:DOD407 2.4 17.4 1.0 D1 A:DOD463 2.7 20.8 1.0 D1 A:DOD407 2.8 23.0 1.0 D2 A:DOD407 3.0 21.6 1.0 D2 A:DOD463 3.2 20.8 1.0 HA A:VAL76 3.3 19.9 1.0 CD A:GLU70 3.3 15.9 1.0 HG2 A:GLU80 3.4 22.8 1.0 D A:GLU77 3.4 19.9 1.0 H A:GLU77 3.4 19.9 0.0 CD A:GLU80 3.4 17.0 1.0 C A:VAL75 3.4 16.4 1.0 C A:ASN72 3.5 15.1 1.0 HA A:ILE73 3.5 17.1 1.0 H A:VAL75 3.5 18.3 0.0 D A:VAL75 3.5 18.3 1.0 HG3 A:GLU77 3.6 22.4 1.0 H A:ASP71 3.7 17.2 0.0 D A:ASP71 3.7 17.2 1.0 HG3 A:GLU80 3.7 22.8 1.0 CG A:GLU80 3.8 20.1 1.0 OE2 A:GLU70 3.8 18.1 1.0 HA A:GLU70 3.8 16.8 1.0 CA A:VAL76 4.1 17.8 1.0 HB3 A:ASN72 4.1 18.7 1.0 N A:GLU77 4.2 17.8 1.0 N A:VAL76 4.2 17.7 1.0 HB2 A:GLU77 4.2 21.9 1.0 H A:ASN72 4.2 17.1 0.1 D A:ASN72 4.2 17.1 0.9 N A:VAL75 4.3 16.5 1.0 OE1 A:GLU77 4.3 19.0 1.0 CA A:ILE73 4.3 15.6 1.0 N A:ILE73 4.3 15.3 1.0 N A:ASN72 4.4 15.5 1.0 CA A:VAL75 4.5 16.9 1.0 CA A:ASN72 4.5 15.5 1.0 CG A:GLU77 4.5 19.8 1.0 O A:DOD459 4.5 20.1 1.0 OE1 A:GLU80 4.5 18.3 1.0 HB3 A:GLU70 4.5 17.3 1.0 C A:ILE73 4.6 15.5 1.0 N A:ASP71 4.6 15.5 1.0 HB A:VAL75 4.6 20.2 1.0 CG A:GLU70 4.6 16.1 1.0 D2 A:DOD442 4.6 19.7 1.0 C A:VAL76 4.7 18.4 1.0 D1 A:DOD459 4.7 25.3 1.0 CA A:GLU70 4.7 15.3 1.0 HG21 A:VAL76 4.7 26.0 1.0 CB A:GLU77 4.8 19.5 1.0 CB A:GLU70 4.8 15.6 1.0 CB A:ASN72 4.8 16.8 1.0 CD A:GLU77 4.8 20.4 1.0 O A:DOD547 4.9 39.1 1.0 N A:ASN74 4.9 15.5 1.0 H A:ASN74 4.9 17.1 0.0 D A:ASN74 4.9 17.1 1.0 HZ A:PHE82 4.9 28.2 1.0 O A:ILE73 5.0 17.1 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