Calcium in PDB 4niw: Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form

All present enzymatic activity of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form:
3.4.21.4;

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, PDB code: 4niw was solved by M.Schoepfel, C.Parthier, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.06 / 1.31
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.522, 58.607, 66.831, 90.00, 90.00, 90.00
R / Rfree (%)	12.8 / 15.5

The binding sites of Calcium atom in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form (pdb code 4niw). 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 Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, PDB code: 4niw:

Calcium binding site 1 out of 1 in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:6.2 occ:1.00 OE1 A:GLU70 2.3 7.2 1.0 O A:VAL75 2.3 6.8 1.0 OE2 A:GLU80 2.4 7.9 1.0 O A:ASN72 2.4 6.6 1.0 O A:HOH418 2.4 8.3 1.0 O A:HOH404 2.4 7.7 1.0 CD A:GLU70 3.4 6.2 1.0 CD A:GLU80 3.4 7.3 1.0 C A:VAL75 3.4 6.5 1.0 C A:ASN72 3.5 5.9 1.0 OE2 A:GLU70 3.8 7.0 1.0 CG A:GLU80 3.8 8.9 1.0 CA A:VAL76 4.1 7.6 1.0 N A:GLU77 4.2 7.8 1.0 N A:VAL76 4.2 6.8 1.0 N A:VAL75 4.2 6.3 1.0 OE1 A:GLU77 4.2 8.8 1.0 CA A:ILE73 4.3 6.2 1.0 N A:ILE73 4.4 5.4 1.0 N A:ASN72 4.4 6.5 1.0 CA A:VAL75 4.4 6.5 1.0 CA A:ASN72 4.5 6.3 1.0 O A:HOH403 4.5 8.8 1.0 CG A:GLU77 4.5 9.2 1.0 N A:ASP71 4.5 7.3 1.0 C A:ILE73 4.5 5.6 1.0 OE1 A:GLU80 4.5 8.4 1.0 C A:VAL76 4.6 8.1 1.0 CG A:GLU70 4.7 6.7 1.0 CA A:GLU70 4.7 6.7 1.0 CD A:GLU77 4.8 9.9 1.0 CB A:GLU77 4.8 8.7 1.0 CB A:GLU70 4.8 5.9 1.0 N A:ASN74 4.9 5.4 1.0 O A:HOH438 4.9 13.4 1.0 O A:ILE73 4.9 6.4 1.0 CB A:ASN72 4.9 7.2 1.0 C A:ASP71 5.0 6.8 1.0

S.Liebscher, M.Schopfel, T.Aumuller, A.Sharkhuukhen, A.Pech, E.Hoss, C.Parthier, G.Jahreis, M.T.Stubbs, F.Bordusa. N-Terminal Protein Modification By Substrate-Activated Reverse Proteolysis. Angew.Chem.Int.Ed.Engl. V. 53 3024 2014.
ISSN: ISSN 1433-7851
PubMed: 24520050
DOI: 10.1002/ANIE.201307736