Calcium in PDB 4y0z: Trypsin in Complex with with Bpti Mutant Aminobutyric Acid

All present enzymatic activity of Trypsin in Complex with with Bpti Mutant Aminobutyric Acid:
3.4.21.4;

The structure of Trypsin in Complex with with Bpti Mutant Aminobutyric Acid, PDB code: 4y0z was solved by B.Loll, S.Ye, A.A.Berger, U.Muelow, C.Alings, M.C.Wahl, B.Koksch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.23 / 1.37
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.907, 82.299, 123.352, 90.00, 90.00, 90.00
R / Rfree (%)	13.4 / 15.6

The binding sites of Calcium atom in the Trypsin in Complex with with Bpti Mutant Aminobutyric Acid (pdb code 4y0z). 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 Trypsin in Complex with with Bpti Mutant Aminobutyric Acid, PDB code: 4y0z:

Calcium binding site 1 out of 1 in the Trypsin in Complex with with Bpti Mutant Aminobutyric Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Trypsin in Complex with with Bpti Mutant Aminobutyric Acid within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca308 b:22.4 occ:1.00 O E:VAL75 2.2 26.9 1.0 OE2 E:GLU70 2.3 20.3 1.0 O E:ASN72 2.3 20.8 1.0 OE2 E:GLU80 2.4 21.9 1.0 O E:HOH460 2.4 21.9 1.0 O E:HOH409 2.4 23.2 1.0 C E:VAL75 2.8 25.5 1.0 HG2 E:GLU80 3.4 25.8 1.0 CD E:GLU70 3.4 18.5 1.0 CD E:GLU80 3.4 21.8 1.0 HA E:VAL76 3.4 37.8 1.0 H E:GLU77 3.5 39.0 1.0 C E:ASN72 3.5 20.2 1.0 HA E:ILE73 3.6 25.5 0.7 HA E:ILE73 3.6 25.7 0.3 HG3 E:GLU77 3.6 38.2 1.0 H E:VAL75 3.7 30.2 1.0 N E:VAL76 3.7 30.4 1.0 OE1 E:GLU70 3.8 18.1 1.0 CG E:GLU80 3.8 21.5 1.0 HG3 E:GLU80 3.8 25.8 1.0 H E:ASP71 3.8 21.4 1.0 HB3 E:ASN72 4.0 24.3 1.0 HA E:GLU70 4.0 20.8 1.0 CA E:VAL76 4.0 31.5 1.0 HB2 E:GLU77 4.0 38.9 1.0 N E:GLU77 4.1 32.5 1.0 CA E:VAL75 4.1 26.1 1.0 N E:VAL75 4.2 25.2 1.0 H E:ASN72 4.2 23.7 1.0 OE1 E:GLU77 4.2 29.2 1.0 CA E:ILE73 4.3 21.3 0.7 CA E:ILE73 4.3 21.4 0.3 N E:ILE73 4.4 20.2 1.0 N E:ASN72 4.4 19.8 1.0 CA E:ASN72 4.4 19.6 1.0 CG E:GLU77 4.4 31.9 1.0 H E:VAL76 4.5 36.5 1.0 OE1 E:GLU80 4.5 23.7 1.0 C E:VAL76 4.5 32.6 1.0 O E:HOH505 4.5 28.4 1.0 HB E:VAL75 4.5 32.8 1.0 C E:ILE73 4.6 21.7 1.0 HB3 E:GLU70 4.6 20.1 1.0 N E:ASP71 4.6 17.9 1.0 CB E:GLU77 4.6 32.4 1.0 CB E:ASN72 4.7 20.2 1.0 CG E:GLU70 4.7 17.2 1.0 HA E:VAL75 4.8 31.3 1.0 CD E:GLU77 4.8 31.2 1.0 O E:HOH562 4.8 30.1 1.0 CA E:GLU70 4.8 17.3 1.0 O E:ILE73 4.9 21.8 1.0 CB E:VAL75 4.9 27.3 1.0 CB E:GLU70 4.9 16.8 1.0 N E:ASN74 5.0 22.2 1.0 CA E:GLU77 5.0 33.7 1.0

S.Ye, B.Loll, A.A.Berger, U.Mulow, C.Alings, M.C.Wahl, B.Koksch. Fluorine Teams Up with Water to Restore Inhibitor Activity to Mutant Bpti. Chem Sci V. 6 5246 2015.
ISSN: ISSN 2041-6520
PubMed: 29449928
DOI: 10.1039/C4SC03227F