Atomistry » Calcium » PDB 2dcj-2dw0 » 2ddf
Atomistry »
  Calcium »
    PDB 2dcj-2dw0 »
      2ddf »

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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2ddf:

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

Zinc (Zn) 2 atoms

Calcium Binding Sites:

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 2ddf

Go back to Calcium Binding Sites List in 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

Reference:

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
Page generated: Sat Dec 12 03:34:58 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy