Calcium in PDB 2ddf: Crystal Structure of Tace in Complex with Tapi-2

All present enzymatic activity of Crystal Structure of Tace in Complex with Tapi-2:
3.4.24.86;

The structure of Crystal Structure of Tace in Complex with Tapi-2, PDB code: 2ddf was solved by P.Orth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.394, 75.639, 103.713, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 23

The structure of Crystal Structure of Tace in Complex with Tapi-2 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Tace in Complex with Tapi-2 (pdb code 2ddf). 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 Tace in Complex with Tapi-2, PDB code: 2ddf:

Calcium binding site 1 out of 1 in the Crystal Structure of Tace in Complex with Tapi-2


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 Tace in Complex with Tapi-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca475 b:35.7 occ:1.00 OD1 A:ASP342 2.3 27.5 1.0 OD1 A:ASN389 2.3 24.9 1.0 O A:PHE343 2.3 26.5 1.0 O A:HOH660 2.4 28.4 1.0 O A:HOH659 2.4 25.9 1.0 N A:PHE343 3.3 26.4 1.0 C A:PHE343 3.3 26.9 1.0 CG A:ASN389 3.5 27.5 1.0 CG A:ASP342 3.5 28.0 1.0 C A:ASP342 3.5 27.0 1.0 CA A:ASP342 3.8 27.0 1.0 CA A:PHE343 3.8 26.4 1.0 O A:THR347 3.8 26.2 1.0 CA A:ASN389 3.9 25.8 1.0 N A:GLY346 3.9 29.2 1.0 CA A:GLY346 4.0 27.6 1.0 N A:TYR390 4.0 27.2 1.0 O A:ASP342 4.1 26.8 1.0 C A:GLY346 4.2 26.8 1.0 CB A:ASP342 4.2 27.5 1.0 CB A:ASN389 4.2 26.8 1.0 N A:THR347 4.2 26.2 1.0 O A:HOH603 4.2 36.5 1.0 CB A:PHE343 4.3 26.3 1.0 O A:LYS388 4.3 24.8 1.0 OD2 A:ASP342 4.4 26.1 1.0 ND2 A:ASN389 4.5 26.6 1.0 N A:ASP344 4.5 29.5 1.0 C A:ASN389 4.5 25.7 1.0 O A:HOH568 4.6 38.1 1.0 C A:THR347 4.7 26.5 1.0 O A:GLY346 4.8 26.4 1.0 C A:ASP344 4.8 30.9 1.0 O A:ASP344 5.0 30.2 1.0 N A:ASN389 5.0 25.2 1.0 CA A:ASP344 5.0 30.2 1.0

R.N.Ingram, P.Orth, C.L.Strickland, H.V.Le, V.Madison, B.M.Beyer. Stabilization of the Autoproteolysis of Tnf-Alpha Converting Enzyme (Tace) Results in A Novel Crystal Form Suitable For Structure-Based Drug Design Studies. Protein Eng.Des.Sel. V. 19 155 2006.
ISSN: ISSN 1741-0126
PubMed: 16459338
DOI: 10.1093/PROTEIN/GZJ014