Calcium in PDB 2fmj: 220-Loop Mutant of Streptomyces Griseus Trypsin

All present enzymatic activity of 220-Loop Mutant of Streptomyces Griseus Trypsin:
3.4.21.4;

The structure of 220-Loop Mutant of Streptomyces Griseus Trypsin, PDB code: 2fmj was solved by M.J.Page, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.58 / 1.65
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	58.319, 58.319, 100.337, 90.00, 90.00, 120.00
R / Rfree (%)	15.7 / 18.9

The binding sites of Calcium atom in the 220-Loop Mutant of Streptomyces Griseus Trypsin (pdb code 2fmj). 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 220-Loop Mutant of Streptomyces Griseus Trypsin, PDB code: 2fmj:

Calcium binding site 1 out of 1 in the 220-Loop Mutant of Streptomyces Griseus Trypsin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 220-Loop Mutant of Streptomyces Griseus Trypsin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca338 b:15.0 occ:1.00 O A:ALA177A 2.4 17.7 1.0 O A:GLU180 2.4 14.1 1.0 OE2 A:GLU230 2.4 22.3 1.0 O A:HOH375 2.5 19.4 1.0 OD2 A:ASP165 2.6 20.7 1.0 OD1 A:ASP165 2.6 17.6 1.0 O A:HOH409 2.6 28.4 1.0 CG A:ASP165 2.9 19.9 1.0 CD A:GLU230 3.5 17.4 1.0 C A:GLU180 3.5 14.1 1.0 C A:ALA177A 3.6 17.4 1.0 OE1 A:GLU230 3.9 15.8 1.0 O A:HOH499 4.1 29.1 1.0 O A:HOH535 4.1 16.4 1.0 CA A:ILE181 4.2 11.3 1.0 N A:ILE181 4.3 13.1 1.0 CA A:ALA177A 4.3 19.0 1.0 N A:GLU180 4.3 12.7 1.0 CB A:ASP165 4.4 19.0 1.0 O A:HOH462 4.5 21.1 1.0 O A:HOH500 4.5 34.6 1.0 N A:ASN178 4.5 17.2 1.0 CA A:GLU180 4.5 13.1 1.0 CA A:ASN178 4.5 16.7 1.0 CB A:ILE181 4.8 12.2 1.0 C A:ASN178 4.8 15.9 1.0 CG A:GLU230 4.8 15.1 1.0 CB A:ALA177A 4.8 21.4 1.0 O A:HOH505 4.9 34.0 1.0 N A:GLU179 4.9 15.4 1.0 CB A:GLU230 4.9 13.8 1.0

M.J.Page, M.R.Bleackley, S.Wong, R.T.Macgillivray, E.Di Cera. Conversion of Trypsin Into A Na(+)-Activated Enzyme. Biochemistry V. 45 2987 2006.
ISSN: ISSN 0006-2960
PubMed: 16503653
DOI: 10.1021/BI052481A