Calcium in PDB 1auj: Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor

All present enzymatic activity of Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor:
3.4.21.4;

The structure of Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor, PDB code: 1auj was solved by R.Alexander, A.Smallwood, C.Kettner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.000, 58.400, 67.600, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / n/a

The binding sites of Calcium atom in the Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor (pdb code 1auj). 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 Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor, PDB code: 1auj:

Calcium binding site 1 out of 1 in the Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Trypsin Complexed to Meta-Cyano-Benzylic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca246 b:19.4 occ:1.00 O A:ILE73 2.6 14.4 1.0 O A:HOH655 2.6 26.5 1.0 O A:HOH611 2.7 11.3 1.0 O A:HOH614 2.7 18.2 1.0 NH1 A:ARG65A 3.3 13.1 1.0 ND2 A:ASN34 3.8 7.7 1.0 C A:ILE73 3.8 14.1 1.0 O A:HOH610 3.9 9.3 1.0 O A:HOH631 4.0 15.5 1.0 O A:HOH630 4.3 18.7 1.0 CZ A:ARG65A 4.3 11.6 1.0 OD1 A:ASN74 4.3 10.2 1.0 CA A:ASN74 4.7 9.8 1.0 N A:ASN74 4.7 10.4 1.0 CB A:ILE73 4.8 16.7 1.0 CA A:ILE73 4.8 14.0 1.0 NE A:ARG65A 4.9 7.7 1.0 CD A:ARG65A 4.9 8.7 1.0 CG A:ASN34 4.9 10.5 1.0 NH2 A:ARG65A 5.0 11.9 1.0

S.L.Lee, R.S.Alexander, A.Smallwood, R.Trievel, L.Mersinger, P.C.Weber, C.Kettner. New Inhibitors of Thrombin and Other Trypsin-Like Proteases: Hydrogen Bonding of An Aromatic Cyano Group with A Backbone Amide of the P1 Binding Site Replaces Binding of A Basic Side Chain. Biochemistry V. 36 13180 1997.
ISSN: ISSN 0006-2960
PubMed: 9341205
DOI: 10.1021/BI970912M