Calcium in PDB 5moq: Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with Benzamidine

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

The structure of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with Benzamidine, PDB code: 5moq 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 / 0.93
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.901, 58.614, 67.604, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 16.7

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

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


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 Benzamidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:10.8 occ:1.00 OE1 A:GLU70 2.3 12.6 1.0 O A:VAL75 2.3 12.3 1.0 OE2 A:GLU80 2.3 12.2 1.0 O A:ASN72 2.3 11.4 1.0 O A:DOD459 2.3 14.0 1.0 O A:DOD405 2.4 12.7 1.0 D1 A:DOD459 2.8 15.7 1.0 D2 A:DOD405 2.9 16.8 1.0 D1 A:DOD405 3.0 17.8 1.0 D2 A:DOD459 3.2 15.6 1.0 HA A:VAL76 3.3 14.4 1.0 CD A:GLU70 3.3 11.2 1.0 HG2 A:GLU80 3.4 17.5 1.0 D A:GLU77 3.4 14.4 1.0 H A:GLU77 3.4 14.4 0.0 CD A:GLU80 3.4 12.2 1.0 C A:VAL75 3.4 11.7 1.0 C A:ASN72 3.5 10.4 1.0 D A:VAL75 3.5 13.0 1.0 H A:VAL75 3.5 13.0 0.0 HA A:ILE73 3.5 12.0 1.0 HG3 A:GLU77 3.6 17.2 1.0 H A:ASP71 3.7 12.0 0.0 D A:ASP71 3.7 12.0 1.0 HG3 A:GLU80 3.7 17.5 1.0 CG A:GLU80 3.8 15.2 1.0 OE2 A:GLU70 3.8 13.3 1.0 HA A:GLU70 3.8 11.7 1.0 HB3 A:ASN72 4.1 13.4 1.0 CA A:VAL76 4.1 12.9 1.0 N A:GLU77 4.2 12.9 1.0 HB2 A:GLU77 4.2 16.2 1.0 N A:VAL76 4.2 12.7 1.0 D A:ASN72 4.2 11.9 0.9 H A:ASN72 4.2 11.9 0.1 N A:VAL75 4.3 11.6 1.0 OE1 A:GLU77 4.3 14.0 1.0 CA A:ILE73 4.3 10.8 1.0 N A:ILE73 4.3 10.5 1.0 N A:ASN72 4.4 10.7 1.0 HB3 A:GLU70 4.5 11.9 1.0 CA A:ASN72 4.5 10.8 1.0 CA A:VAL75 4.5 12.0 1.0 O A:DOD460 4.5 15.4 1.0 CG A:GLU77 4.5 15.1 1.0 OE1 A:GLU80 4.5 13.4 1.0 C A:ILE73 4.6 10.7 1.0 N A:ASP71 4.6 10.8 1.0 HB A:VAL75 4.6 14.6 1.0 CG A:GLU70 4.6 11.2 1.0 D1 A:DOD447 4.7 14.3 1.0 C A:VAL76 4.7 13.5 1.0 D2 A:DOD460 4.7 20.5 1.0 CA A:GLU70 4.7 10.5 1.0 CB A:GLU77 4.8 14.3 1.0 CB A:GLU70 4.8 10.7 1.0 CB A:ASN72 4.8 11.9 1.0 CD A:GLU77 4.8 15.5 1.0 O A:DOD560 4.9 27.8 1.0 N A:ASN74 4.9 10.7 1.0 HG21 A:VAL76 4.9 19.9 1.0 HZ A:PHE82 4.9 22.5 1.0 H A:ASN74 4.9 11.8 0.0 D A:ASN74 4.9 11.8 1.0 O A:ILE73 5.0 12.4 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