Calcium in PDB 5mnx: Neutron Structure of Cationic Trypsin in Complex with 2-Aminopyridine

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

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

Calcium binding site 1 out of 1 in the 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 Neutron Structure of Cationic Trypsin in Complex with 2-Aminopyridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:8.7 occ:1.00 O A:VAL75 2.2 11.4 1.0 O A:DOD453 2.3 14.1 1.0 OE1 A:GLU70 2.3 11.4 1.0 O A:ASN72 2.3 10.2 1.0 OE2 A:GLU80 2.4 13.5 1.0 O A:DOD410 2.4 13.5 1.0 D1 A:DOD453 2.6 14.2 1.0 D1 A:DOD410 2.9 16.3 1.0 D2 A:DOD410 3.0 14.7 1.0 D2 A:DOD453 3.1 16.8 1.0 HA A:VAL76 3.2 16.4 1.0 HG2 A:GLU80 3.3 15.2 1.0 CD A:GLU70 3.4 10.1 1.0 C A:VAL75 3.4 11.5 1.0 H A:GLU77 3.4 13.5 0.1 D A:GLU77 3.4 13.5 0.9 CD A:GLU80 3.4 14.5 1.0 C A:ASN72 3.5 11.6 1.0 HA A:ILE73 3.5 11.9 1.0 HG3 A:GLU77 3.5 14.5 1.0 D A:VAL75 3.5 14.8 1.0 H A:VAL75 3.5 14.8 0.0 D A:ASP71 3.7 11.4 1.0 H A:ASP71 3.7 11.4 0.0 CG A:GLU80 3.7 13.3 1.0 OE2 A:GLU70 3.8 12.4 1.0 HG3 A:GLU80 3.8 17.0 1.0 HA A:GLU70 3.8 14.1 1.0 HB3 A:ASN72 4.1 12.3 1.0 CA A:VAL76 4.1 12.1 1.0 N A:VAL76 4.2 12.1 1.0 N A:GLU77 4.2 13.1 1.0 N A:VAL75 4.2 11.4 1.0 H A:ASN72 4.2 12.3 0.0 D A:ASN72 4.2 12.3 1.0 CA A:ILE73 4.3 10.4 1.0 N A:ILE73 4.3 10.4 1.0 OE1 A:GLU77 4.3 16.1 1.0 HB2 A:GLU77 4.4 19.6 1.0 N A:ASN72 4.4 10.6 1.0 CA A:VAL75 4.4 12.7 1.0 CA A:ASN72 4.5 10.8 1.0 CG A:GLU77 4.5 16.4 1.0 OE1 A:GLU80 4.5 11.8 1.0 HB3 A:GLU70 4.5 10.0 1.0 C A:ILE73 4.6 11.1 1.0 D2 A:DOD425 4.6 13.3 1.0 C A:VAL76 4.6 16.0 1.0 N A:ASP71 4.6 10.9 1.0 HB A:VAL75 4.6 17.1 1.0 CG A:GLU70 4.6 10.9 1.0 D1 A:DOD467 4.7 18.2 1.0 CA A:GLU70 4.8 9.8 1.0 HG22 A:VAL76 4.8 18.5 1.0 O A:DOD467 4.8 16.4 1.0 CB A:ASN72 4.8 9.1 1.0 HZ A:PHE82 4.8 20.7 1.0 CD A:GLU77 4.9 17.9 1.0 N A:ASN74 4.9 10.8 1.0 CB A:GLU77 4.9 15.8 1.0 CB A:GLU70 4.9 9.0 1.0 O A:DOD532 4.9 26.8 1.0 D A:ASN74 4.9 10.6 1.0 H A:ASN74 4.9 10.6 0.0 O A:ILE73 5.0 14.2 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