Calcium in PDB 5mo2: Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine

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

The binding sites of Calcium atom in the Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine (pdb code 5mo2). 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 N- Amidinopiperidine, PDB code: 5mo2:

Calcium binding site 1 out of 1 in the Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine


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 N- Amidinopiperidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:8.0 occ:1.00 O A:VAL75 2.2 10.6 1.0 O A:DOD409 2.3 9.4 1.0 OE1 A:GLU70 2.3 9.5 1.0 O A:ASN72 2.3 7.7 1.0 OE2 A:GLU80 2.4 9.4 1.0 O A:DOD456 2.4 10.7 1.0 D1 A:DOD409 2.8 11.4 1.0 D2 A:DOD456 2.8 12.0 1.0 D2 A:DOD409 2.9 12.4 1.0 D1 A:DOD456 3.2 12.2 1.0 HA A:VAL76 3.2 10.1 1.0 HG2 A:GLU80 3.3 12.1 1.0 H A:GLU77 3.4 10.1 0.0 D A:GLU77 3.4 10.1 1.0 C A:VAL75 3.4 8.6 1.0 CD A:GLU70 3.4 8.0 1.0 CD A:GLU80 3.4 9.3 1.0 D A:VAL75 3.5 9.9 0.9 H A:VAL75 3.5 9.9 0.1 C A:ASN72 3.5 8.5 1.0 HG3 A:GLU77 3.5 10.3 1.0 HA A:ILE73 3.6 7.3 1.0 H A:ASP71 3.7 9.4 0.0 D A:ASP71 3.7 9.4 1.0 CG A:GLU80 3.7 11.0 1.0 HG3 A:GLU80 3.7 13.3 1.0 OE2 A:GLU70 3.8 8.7 1.0 HA A:GLU70 3.8 11.0 1.0 HB3 A:ASN72 4.1 8.4 1.0 CA A:VAL76 4.1 10.3 1.0 N A:GLU77 4.1 8.7 1.0 D A:ASN72 4.1 10.0 1.0 H A:ASN72 4.1 10.0 0.0 N A:VAL76 4.2 10.3 1.0 OE1 A:GLU77 4.2 12.1 1.0 N A:VAL75 4.2 6.8 1.0 CA A:ILE73 4.3 8.7 1.0 N A:ILE73 4.4 8.1 1.0 N A:ASN72 4.4 8.0 1.0 CA A:VAL75 4.4 8.8 1.0 CG A:GLU77 4.5 11.9 1.0 CA A:ASN72 4.5 6.8 1.0 HB3 A:GLU70 4.5 7.3 1.0 OE1 A:GLU80 4.5 8.6 1.0 C A:ILE73 4.6 8.9 1.0 O A:DOD484 4.6 13.4 1.0 HB A:VAL75 4.6 13.1 1.0 C A:VAL76 4.6 12.0 1.0 N A:ASP71 4.6 6.9 1.0 D2 A:DOD484 4.6 11.9 1.0 CG A:GLU70 4.7 7.4 1.0 D1 A:DOD447 4.7 12.0 1.0 CA A:GLU70 4.7 7.8 1.0 CB A:GLU77 4.8 8.7 1.0 HG21 A:VAL76 4.8 17.0 1.0 CD A:GLU77 4.8 13.0 1.0 CB A:ASN72 4.8 6.9 1.0 CB A:GLU70 4.9 6.4 1.0 N A:ASN74 4.9 6.7 1.0 D A:ASN74 5.0 10.5 1.0 H A:ASN74 5.0 10.5 0.0 O A:DOD534 5.0 19.1 1.0 O A:ILE73 5.0 9.5 1.0

J.Schiebel, R.Gaspari, T.Wulsdorf, K.Ngo, C.Sohn, T.E.Schrader, A.Cavalli, A.Ostermann, A.Heine, G.Klebe. Intriguing Role of Water in Protein-Ligand Binding Studied By Neutron Crystallography on Trypsin Complexes. Nat Commun V. 9 3559 2018.
ISSN: ESSN 2041-1723
PubMed: 30177695
DOI: 10.1038/S41467-018-05769-2