Calcium in PDB 5mnn: Cationic Trypsin in Complex with N-Amidinopiperidine (Deuterated Sample at 100 K)

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

The structure of Cationic Trypsin in Complex with N-Amidinopiperidine (Deuterated Sample at 100 K), PDB code: 5mnn 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)	39.86 / 0.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.680, 58.222, 66.849, 90.00, 90.00, 90.00
R / Rfree (%)	10 / 11

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

Calcium binding site 1 out of 1 in the Cationic Trypsin in Complex with N-Amidinopiperidine (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 N-Amidinopiperidine (Deuterated Sample at 100 K) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:5.8 occ:1.00 OE1 A:GLU70 2.3 6.6 1.0 O A:VAL75 2.3 6.6 1.0 O A:ASN72 2.3 6.2 1.0 OE2 A:GLU80 2.3 6.5 1.0 O A:HOH535 2.3 7.1 1.0 O A:HOH411 2.4 6.6 1.0 H1 A:HOH411 2.6 7.9 1.0 H1 A:HOH535 2.8 8.6 1.0 H2 A:HOH535 2.9 8.6 1.0 CD A:GLU70 3.3 5.8 1.0 HA A:VAL76 3.4 8.6 1.0 HG2 A:GLU80 3.4 10.2 1.0 CD A:GLU80 3.4 6.6 1.0 C A:VAL75 3.4 6.4 1.0 C A:ASN72 3.5 5.8 1.0 H A:GLU77 3.5 8.6 0.4 H A:GLU77 3.5 8.8 0.6 H A:VAL75 3.5 7.5 1.0 HA A:ILE73 3.6 7.0 1.0 HG3 A:GLU77 3.7 9.9 0.4 HG3 A:GLU80 3.7 10.2 1.0 HG3 A:GLU77 3.7 9.8 0.6 CG A:GLU80 3.7 8.5 1.0 OE2 A:GLU70 3.8 6.7 1.0 H A:ASP71 3.8 7.1 1.0 HA A:GLU70 3.9 6.8 1.0 CA A:VAL76 4.1 7.2 1.0 N A:GLU77 4.2 7.2 0.4 N A:GLU77 4.2 7.3 0.6 N A:VAL76 4.2 6.9 1.0 HB3 A:ASN72 4.2 8.6 1.0 N A:VAL75 4.2 6.2 1.0 OE1 A:GLU77 4.2 8.0 0.6 CA A:ILE73 4.3 5.8 1.0 OE1 A:GLU77 4.3 7.9 0.4 N A:ILE73 4.3 5.9 1.0 N A:ASN72 4.4 6.1 1.0 CA A:VAL75 4.4 6.6 1.0 CA A:ASN72 4.5 6.2 1.0 O A:HOH529 4.5 7.5 1.0 CG A:GLU77 4.5 8.2 0.6 CG A:GLU77 4.5 8.2 0.4 HB3 A:GLU70 4.5 6.9 1.0 OE1 A:GLU80 4.5 7.1 1.0 C A:ILE73 4.5 5.9 1.0 N A:ASP71 4.6 6.0 1.0 CG A:GLU70 4.6 5.8 1.0 HB A:VAL75 4.6 8.7 1.0 C A:VAL76 4.7 7.6 1.0 H1 A:HOH500 4.7 7.9 1.0 CA A:GLU70 4.7 5.6 1.0 CD A:GLU77 4.8 8.5 0.6 CB A:GLU77 4.8 8.4 0.6 CB A:GLU77 4.8 7.5 0.4 O A:HOH652 4.8 11.8 1.0 CB A:GLU70 4.8 5.7 1.0 HG22 A:VAL76 4.8 10.5 1.0 CB A:ASN72 4.8 7.2 1.0 N A:ASN74 4.9 6.0 1.0 CD A:GLU77 4.9 9.3 0.4 H A:ASN74 4.9 7.2 1.0 O A:ILE73 4.9 6.5 1.0 C A:ASP71 5.0 5.9 1.0 HG2 A:GLU70 5.0 7.0 1.0 H A:VAL76 5.0 8.2 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