Zinc in PDB 2fv9: Crystal Structure of Tace in Complex with Jmv 390-1

All present enzymatic activity of Crystal Structure of Tace in Complex with Jmv 390-1:
3.4.24.86;

The structure of Crystal Structure of Tace in Complex with Jmv 390-1, PDB code: 2fv9 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 / 2.02
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.799, 76.221, 102.092, 90.00, 90.00, 90.00
R / Rfree (%)	25.1 / 26.4

The binding sites of Zinc atom in the Crystal Structure of Tace in Complex with Jmv 390-1 (pdb code 2fv9). 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 Jmv 390-1, PDB code: 2fv9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Tace in Complex with Jmv 390-1


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 Jmv 390-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:35.3 occ:1.00 NE2 A:HIS415 2.0 34.2 1.0 O A:INN9 2.1 34.0 1.0 O4 A:INN9 2.1 33.3 1.0 NE2 A:HIS405 2.1 25.3 1.0 NE2 A:HIS409 2.1 25.9 1.0 C A:INN9 2.7 34.6 1.0 N A:INN9 2.8 33.8 1.0 CE1 A:HIS415 3.0 34.6 1.0 CD2 A:HIS409 3.0 26.6 1.0 CE1 A:HIS405 3.1 25.7 1.0 CD2 A:HIS415 3.1 34.5 1.0 CD2 A:HIS405 3.2 25.9 1.0 CE1 A:HIS409 3.2 26.5 1.0 O A:HOH480 3.9 36.5 1.0 ND1 A:HIS415 4.1 34.4 1.0 CG A:HIS415 4.2 34.5 1.0 C0 A:INN9 4.2 35.5 1.0 ND1 A:HIS405 4.2 25.5 1.0 CG A:HIS409 4.2 26.6 1.0 O A:HOH483 4.2 29.3 1.0 ND1 A:HIS409 4.3 26.4 1.0 CG A:HIS405 4.3 25.7 1.0 OE1 A:GLU406 4.5 27.0 1.0 CA A:INN9 4.8 36.8 1.0 CB A:INN9 4.8 36.4 1.0 OE2 A:GLU406 4.9 27.5 1.0 CE A:MET435 5.0 33.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Tace in Complex with Jmv 390-1


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 Jmv 390-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4 b:37.2 occ:1.00 O3 B:0022 2.0 34.5 1.0 O2 B:0022 2.0 34.4 1.0 NE2 B:HIS405 2.1 26.8 1.0 NE2 B:HIS409 2.1 29.5 1.0 NE2 B:HIS415 2.2 32.4 1.0 C9 B:0022 2.7 35.3 1.0 N1 B:0022 2.9 35.3 1.0 CD2 B:HIS409 3.0 29.0 1.0 CD2 B:HIS405 3.1 26.5 1.0 CE1 B:HIS405 3.1 26.6 1.0 CE1 B:HIS415 3.1 32.8 1.0 CD2 B:HIS415 3.1 32.4 1.0 CE1 B:HIS409 3.2 29.3 1.0 O B:HOH528 3.8 45.0 1.0 C10 B:0022 4.2 35.9 1.0 ND1 B:HIS405 4.2 26.1 1.0 CG B:HIS409 4.2 29.1 1.0 CG B:HIS405 4.2 26.4 1.0 ND1 B:HIS409 4.2 29.2 1.0 ND1 B:HIS415 4.3 32.7 1.0 CG B:HIS415 4.3 32.9 1.0 OE1 B:GLU406 4.5 29.0 1.0 OE2 B:GLU406 4.6 28.8 1.0 CE B:MET435 4.7 33.1 1.0 C22 B:0022 4.8 36.8 1.0 C23 B:0022 4.9 36.2 1.0 CD B:GLU406 4.9 28.8 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