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

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

The structure of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with Aniline, PDB code: 5moo 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 / 1.44
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.875, 58.472, 67.458, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 18.5

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

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


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 Aniline within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:19.6 occ:1.00 OE1 A:GLU70 2.2 21.6 1.0 O A:VAL75 2.3 20.4 1.0 O A:DOD443 2.3 22.1 1.0 O A:ASN72 2.3 20.0 1.0 OE2 A:GLU80 2.3 21.1 1.0 O A:DOD401 2.4 21.2 1.0 D1 A:DOD443 2.7 21.1 1.0 D2 A:DOD401 2.9 24.0 1.0 D1 A:DOD401 3.0 25.0 1.0 D2 A:DOD443 3.1 27.9 1.0 HA A:VAL76 3.2 22.5 1.0 CD A:GLU70 3.3 19.8 1.0 H A:GLU77 3.3 24.1 0.0 D A:GLU77 3.3 24.1 1.0 HG2 A:GLU80 3.4 24.3 1.0 CD A:GLU80 3.4 22.2 1.0 C A:VAL75 3.4 19.4 1.0 C A:ASN72 3.5 19.0 1.0 D A:VAL75 3.5 19.4 0.9 H A:VAL75 3.5 19.4 0.1 HA A:ILE73 3.5 18.3 1.0 HG3 A:GLU77 3.5 28.5 1.0 D A:ASP71 3.7 18.6 1.0 H A:ASP71 3.7 18.6 0.0 CG A:GLU80 3.7 22.4 1.0 OE2 A:GLU70 3.7 21.6 1.0 HG3 A:GLU80 3.7 24.3 1.0 HA A:GLU70 3.8 17.6 1.0 HB3 A:ASN72 4.1 19.1 1.0 CA A:VAL76 4.1 21.4 1.0 N A:GLU77 4.1 22.4 1.0 N A:VAL76 4.2 20.6 1.0 HB2 A:GLU77 4.2 26.1 1.0 H A:ASN72 4.2 18.1 0.1 D A:ASN72 4.2 18.1 0.9 N A:VAL75 4.3 19.2 1.0 OE1 A:GLU77 4.3 22.9 1.0 CA A:ILE73 4.3 18.4 1.0 N A:ILE73 4.3 18.8 1.0 N A:ASN72 4.4 17.7 1.0 CA A:VAL75 4.5 20.4 1.0 CA A:ASN72 4.5 18.7 1.0 HB3 A:GLU70 4.5 19.0 1.0 CG A:GLU77 4.5 25.8 1.0 O A:DOD440 4.5 24.5 1.0 OE1 A:GLU80 4.5 22.6 1.0 C A:ILE73 4.6 19.4 1.0 HB A:VAL75 4.6 23.1 1.0 N A:ASP71 4.6 18.2 1.0 CG A:GLU70 4.6 19.3 1.0 C A:VAL76 4.6 22.5 1.0 D2 A:DOD440 4.7 31.8 1.0 D1 A:DOD435 4.7 22.5 1.0 CA A:GLU70 4.7 17.7 1.0 CB A:GLU77 4.8 23.9 1.0 HG22 A:VAL76 4.8 30.8 1.0 O A:DOD539 4.8 35.0 1.0 CB A:GLU70 4.8 18.7 1.0 CD A:GLU77 4.8 27.0 1.0 CB A:ASN72 4.8 19.1 1.0 HZ A:PHE82 4.9 31.7 1.0 N A:ASN74 4.9 18.3 1.0 O A:ILE73 4.9 20.9 1.0 D A:ASN74 5.0 18.2 1.0 H A:ASN74 5.0 18.2 0.0

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