Zinc 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:

Calcium

(Ca)

1 atom

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Tace in Complex with Tapi-2, PDB code: 2ddf:
Jump to Zinc binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn1 b:29.5 occ:1.00 NE2 A:HIS415 2.0 25.0 1.0 O A:INN3 2.1 25.4 1.0 NE2 A:HIS405 2.1 26.4 1.0 NE2 A:HIS409 2.1 26.2 1.0 O4 A:INN3 2.2 26.1 1.0 O A:HOH661 2.5 32.6 1.0 C A:INN3 2.7 23.6 1.0 N A:INN3 2.8 26.1 1.0 CD2 A:HIS405 3.0 24.6 1.0 CD2 A:HIS409 3.0 25.7 1.0 CE1 A:HIS415 3.0 27.3 1.0 CD2 A:HIS415 3.0 28.1 1.0 CE1 A:HIS405 3.1 24.0 1.0 CE1 A:HIS409 3.1 29.3 1.0 O A:HOH663 4.0 29.2 1.0 ND1 A:HIS415 4.1 28.3 1.0 C0 A:INN3 4.2 24.6 1.0 CG A:HIS415 4.2 27.5 1.0 CG A:HIS405 4.2 23.7 1.0 ND1 A:HIS405 4.2 25.6 1.0 CG A:HIS409 4.2 26.5 1.0 ND1 A:HIS409 4.2 26.4 1.0 OE1 A:GLU406 4.4 25.8 1.0 O A:HOH642 4.5 28.1 1.0 O A:HOH664 4.5 41.8 1.0 CA A:INN3 4.7 24.3 1.0 CE A:MET435 4.7 27.9 1.0 CB A:INN3 4.9 25.7 1.0 OE2 A:GLU406 4.9 26.6 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Tace in Complex with Tapi-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4 b:31.2 occ:1.00 O4 B:INN2 2.1 27.9 1.0 NE2 B:HIS415 2.1 26.8 1.0 O B:INN2 2.1 28.1 1.0 NE2 B:HIS409 2.1 27.8 1.0 NE2 B:HIS405 2.1 27.5 1.0 O B:HOH642 2.5 39.0 1.0 C B:INN2 2.8 30.0 1.0 N B:INN2 2.8 31.6 1.0 CE1 B:HIS415 3.0 30.4 1.0 CD2 B:HIS409 3.0 27.9 1.0 CD2 B:HIS415 3.1 26.8 1.0 CD2 B:HIS405 3.1 26.7 1.0 CE1 B:HIS405 3.1 25.8 1.0 CE1 B:HIS409 3.2 29.4 1.0 O B:HOH645 4.0 34.6 1.0 ND1 B:HIS415 4.1 28.5 1.0 CG B:HIS415 4.2 27.2 1.0 CG B:HIS409 4.2 27.2 1.0 C0 B:INN2 4.2 30.2 1.0 ND1 B:HIS405 4.2 27.0 1.0 ND1 B:HIS409 4.2 27.7 1.0 CG B:HIS405 4.2 25.1 1.0 OE1 B:GLU406 4.4 28.6 1.0 O B:HOH630 4.5 32.1 1.0 O B:HOH599 4.5 44.2 1.0 CA B:INN2 4.6 29.9 1.0 CB B:INN2 4.7 30.5 1.0 CE B:MET435 4.7 29.6 1.0 OE2 B:GLU406 4.9 28.2 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