Calcium in PDB 5mos: Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine

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

The structure of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine, PDB code: 5mos 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 / 0.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.903, 58.646, 67.615, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 18

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

Calcium binding site 1 out of 1 in the Joint X-Ray/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 Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:13.2 occ:1.00 OE1 A:GLU70 2.3 14.9 1.0 O A:VAL75 2.3 14.5 1.0 OE2 A:GLU80 2.3 14.6 1.0 O A:ASN72 2.3 13.8 1.0 O A:DOD451 2.3 16.4 1.0 O A:DOD405 2.4 14.9 1.0 D1 A:DOD405 2.8 17.0 1.0 D2 A:DOD451 2.8 20.6 1.0 D2 A:DOD405 2.9 19.2 1.0 D1 A:DOD451 3.1 17.7 1.0 HA A:VAL76 3.2 17.0 1.0 CD A:GLU70 3.3 13.3 1.0 D A:GLU77 3.3 17.2 1.0 H A:GLU77 3.3 17.2 0.0 HG2 A:GLU80 3.4 19.3 1.0 CD A:GLU80 3.4 14.3 1.0 C A:VAL75 3.4 13.8 1.0 H A:VAL75 3.5 15.3 0.1 D A:VAL75 3.5 15.3 0.9 C A:ASN72 3.5 12.7 1.0 HA A:ILE73 3.5 14.6 1.0 HG3 A:GLU77 3.6 19.2 1.0 D A:ASP71 3.7 14.4 1.0 H A:ASP71 3.7 14.4 0.0 HG3 A:GLU80 3.8 19.3 1.0 CG A:GLU80 3.8 17.0 1.0 OE2 A:GLU70 3.8 15.4 1.0 HA A:GLU70 3.8 14.3 1.0 HB3 A:ASN72 4.1 16.2 1.0 CA A:VAL76 4.1 15.2 1.0 N A:GLU77 4.2 15.3 1.0 D A:ASN72 4.2 14.5 0.9 H A:ASN72 4.2 14.5 0.1 N A:VAL76 4.2 15.0 1.0 N A:VAL75 4.3 13.8 1.0 OE1 A:GLU77 4.3 16.2 1.0 CA A:ILE73 4.3 13.1 1.0 N A:ILE73 4.3 12.8 1.0 N A:ASN72 4.4 13.1 1.0 CA A:VAL75 4.5 14.3 1.0 CA A:ASN72 4.5 13.1 1.0 HB3 A:GLU70 4.5 14.6 1.0 CG A:GLU77 4.5 17.0 1.0 O A:DOD458 4.5 17.4 1.0 OE1 A:GLU80 4.5 15.6 1.0 C A:ILE73 4.6 13.1 1.0 N A:ASP71 4.6 13.0 1.0 HB A:VAL75 4.6 17.5 1.0 CG A:GLU70 4.6 13.6 1.0 C A:VAL76 4.6 15.8 1.0 D1 A:DOD441 4.7 22.0 1.0 CA A:GLU70 4.7 12.9 1.0 HG21 A:VAL76 4.7 22.2 1.0 D2 A:DOD458 4.7 23.4 1.0 CB A:GLU77 4.8 16.8 1.0 CB A:GLU70 4.8 13.1 1.0 CD A:GLU77 4.8 17.8 1.0 CB A:ASN72 4.8 14.4 1.0 O A:DOD551 4.9 28.0 1.0 N A:ASN74 4.9 13.0 1.0 H A:ASN74 4.9 14.3 0.0 D A:ASN74 4.9 14.3 1.0 O A:ILE73 5.0 14.7 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