Sodium in PDB 2ftl: Crystal Structure of Trypsin Complexed with Bpti at 100K

All present enzymatic activity of Crystal Structure of Trypsin Complexed with Bpti at 100K:
3.4.21.4;

The structure of Crystal Structure of Trypsin Complexed with Bpti at 100K, PDB code: 2ftl was solved by W.M.Hanson, M.P.Horvath, D.P.Goldenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.62
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.726, 81.906, 124.261, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 22.7

The structure of Crystal Structure of Trypsin Complexed with Bpti at 100K also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of Trypsin Complexed with Bpti at 100K (pdb code 2ftl). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Trypsin Complexed with Bpti at 100K, PDB code: 2ftl:

Sodium binding site 1 out of 1 in the Crystal Structure of Trypsin Complexed with Bpti at 100K


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Trypsin Complexed with Bpti at 100K within 5.0Å range: probe atom residue distance (Å) B Occ E:Na1001 b:48.4 occ:1.00 OD2 E:ASP71 2.4 20.5 1.0 OE2 E:GLU77 2.7 28.3 1.0 O E:HOH1141 3.4 36.3 1.0 CG E:ASP71 3.5 19.1 1.0 CD E:GLU77 3.5 27.9 1.0 OE1 E:GLU77 3.5 26.1 1.0 O E:HOH1193 3.8 39.0 1.0 CG1 E:VAL154 3.9 17.3 1.0 CB E:ASP71 4.0 17.0 1.0 O E:HOH1063 4.2 23.4 1.0 N E:ASN72 4.4 15.4 1.0 O E:HOH1137 4.4 31.9 1.0 CB E:ASN72 4.4 14.9 1.0 CB E:ALA24 4.5 23.1 1.0 OD1 E:ASP71 4.6 19.1 1.0 O E:HOH1143 4.9 33.2 1.0 CA E:ASN72 4.9 15.3 1.0 CG E:GLU77 5.0 27.3 1.0 CB E:VAL154 5.0 17.5 1.0

W.M.Hanson, G.J.Domek, M.P.Horvath, D.P.Goldenberg. Rigidification of A Flexible Protease Inhibitor Variant Upon Binding to Trypsin. J.Mol.Biol. V. 366 230 2007.
ISSN: ISSN 0022-2836
PubMed: 17157870
DOI: 10.1016/J.JMB.2006.11.003