Calcium in PDB 3beu: Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity

All present enzymatic activity of Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity:
3.4.21.4;

The structure of Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity, PDB code: 3beu was solved by M.J.Page, C.J.Carrell, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.786, 72.433, 122.492, 90.00, 90.00, 90.00
R / Rfree (%)	12.1 / 14.6

The structure of Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Calcium atom in the Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity (pdb code 3beu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity, PDB code: 3beu:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca249 b:9.6 occ:1.00 O A:ALA177A 2.3 11.2 1.0 OE1 A:GLU230 2.3 10.7 1.0 O A:MET180 2.3 9.3 1.0 O A:HOH272 2.4 10.8 1.0 O A:HOH279 2.4 12.1 1.0 OD2 A:ASP165 2.4 12.6 1.0 OD1 A:ASP165 2.5 10.3 1.0 CG A:ASP165 2.8 10.2 1.0 C A:ALA177A 3.4 11.1 1.0 CD A:GLU230 3.4 9.6 1.0 C A:MET180 3.5 8.5 1.0 O A:HOH573 3.7 63.6 1.0 OE2 A:GLU230 3.9 10.4 1.0 O A:HOH253 4.1 8.8 1.0 CA A:ALA177A 4.1 12.7 1.0 N A:ILE181 4.2 8.3 1.0 CA A:ILE181 4.2 8.6 1.0 N A:MET180 4.3 8.8 1.0 CB A:ASP165 4.4 11.0 1.0 N A:ASN178 4.5 11.2 1.0 CA A:MET180 4.5 8.6 1.0 O A:HOH299 4.5 14.7 1.0 CA A:ASN178 4.6 11.0 0.4 O A:HOH345 4.7 20.5 1.0 CB A:ALA177A 4.7 17.7 1.0 CA A:ASN178 4.7 12.2 0.6 CB A:ILE181 4.7 10.3 1.0 C A:ASN178 4.7 10.1 1.0 CG A:GLU230 4.7 9.5 1.0 O A:HOH377 4.8 24.3 1.0 O A:HOH365 4.9 23.3 1.0 CB A:GLU230 4.9 8.7 1.0

Calcium binding site 2 out of 2 in the Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca249 b:12.0 occ:1.00 O B:ALA177A 2.3 13.8 1.0 OE1 B:GLU230 2.3 12.0 1.0 O B:MET180 2.3 12.2 1.0 O B:HOH286 2.4 13.9 1.0 O B:HOH280 2.4 13.3 1.0 OD2 B:ASP165 2.4 15.2 1.0 OD1 B:ASP165 2.5 13.8 1.0 CG B:ASP165 2.8 15.1 1.0 CD B:GLU230 3.4 11.5 1.0 C B:ALA177A 3.5 13.9 1.0 C B:MET180 3.5 10.3 1.0 OE2 B:GLU230 3.9 12.9 1.0 O B:HOH270 4.0 12.3 1.0 CA B:ALA177A 4.1 15.1 1.0 CA B:ILE181 4.2 10.7 1.0 N B:ILE181 4.2 10.3 1.0 CB B:ASP165 4.4 16.3 1.0 N B:MET180 4.4 11.1 1.0 O B:HOH310 4.4 16.8 1.0 N B:ASN178 4.5 13.6 1.0 CA B:MET180 4.5 11.2 1.0 O B:HOH377 4.5 27.0 1.0 CA B:ASN178 4.5 14.4 0.4 CA B:ASN178 4.7 13.9 0.6 CB B:ALA177A 4.7 19.1 1.0 CB B:ILE181 4.7 12.2 1.0 CG B:GLU230 4.7 10.9 1.0 C B:ASN178 4.8 12.6 1.0 O B:HOH399 4.9 30.1 1.0 CB B:GLU230 5.0 9.8 1.0

M.J.Page, C.J.Carrell, E.Di Cera. Engineering Protein Allostery: 1.05 A Resolution Structure and Enzymatic Properties of A Na+-Activated Trypsin. J.Mol.Biol. V. 378 666 2008.
ISSN: ISSN 0022-2836
PubMed: 18377928
DOI: 10.1016/J.JMB.2008.03.003