Calcium in PDB 1k1n: Bovine Trypsin-Inhibitor Complex

All present enzymatic activity of Bovine Trypsin-Inhibitor Complex:
3.4.21.4;

The structure of Bovine Trypsin-Inhibitor Complex, PDB code: 1k1n was solved by M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.798, 58.273, 67.277, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / n/a

The binding sites of Calcium atom in the Bovine Trypsin-Inhibitor Complex (pdb code 1k1n). 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-Inhibitor Complex, PDB code: 1k1n:

Calcium binding site 1 out of 1 in the Bovine Trypsin-Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Trypsin-Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca480 b:11.3 occ:1.00 O A:ASN72 2.2 10.2 1.0 O A:VAL75 2.2 12.5 1.0 O A:HOH1031 2.3 12.2 1.0 O A:HOH1034 2.4 16.8 1.0 OE1 A:GLU70 2.4 10.4 1.0 OE2 A:GLU80 2.5 15.4 1.0 C A:VAL75 3.4 11.7 1.0 C A:ASN72 3.4 11.1 1.0 CD A:GLU70 3.5 11.6 1.0 CD A:GLU80 3.6 10.8 1.0 CG A:GLU80 3.9 8.9 1.0 OE2 A:GLU70 4.0 12.7 1.0 OE1 A:GLU77 4.1 15.2 1.0 CA A:VAL76 4.1 12.0 1.0 N A:GLU77 4.1 12.0 1.0 CA A:ILE73 4.2 11.6 1.0 N A:VAL76 4.2 12.7 1.0 N A:VAL75 4.2 10.4 1.0 N A:ILE73 4.2 9.2 1.0 N A:ASN72 4.3 10.0 1.0 CA A:ASN72 4.4 9.8 1.0 CA A:VAL75 4.4 11.9 1.0 CG A:GLU77 4.5 14.8 1.0 C A:ILE73 4.5 11.9 1.0 O A:HOH1027 4.5 8.4 1.0 N A:ASP71 4.5 8.6 1.0 C A:VAL76 4.6 13.5 1.0 OE1 A:GLU80 4.7 9.8 1.0 CD A:GLU77 4.7 19.2 1.0 O A:HOH1053 4.7 30.9 1.0 CG A:GLU70 4.7 10.4 1.0 CB A:ASN72 4.8 8.9 1.0 CA A:GLU70 4.8 10.1 1.0 N A:ASN74 4.8 9.5 1.0 CB A:GLU77 4.8 12.6 1.0 O A:ILE73 4.9 13.1 1.0 CB A:GLU70 4.9 9.3 1.0 C A:ASP71 4.9 10.8 1.0

F.Dullweber, M.T.Stubbs, D.Musil, J.Sturzebecher, G.Klebe. Factorising Ligand Affinity: A Combined Thermodynamic and Crystallographic Study of Trypsin and Thrombin Inhibition. J.Mol.Biol. V. 313 593 2001.
ISSN: ISSN 0022-2836
PubMed: 11676542
DOI: 10.1006/JMBI.2001.5062