Zinc in PDB 2fv5: Crystal Structure of Tace in Complex with IK682

All present enzymatic activity of Crystal Structure of Tace in Complex with IK682:
3.4.24.86;

The structure of Crystal Structure of Tace in Complex with IK682, PDB code: 2fv5 was solved by P.Orth, X.Niu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.614, 75.696, 103.258, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.6

The binding sites of Zinc atom in the Crystal Structure of Tace in Complex with IK682 (pdb code 2fv5). 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 IK682, PDB code: 2fv5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Tace in Complex with IK682


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 IK682 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3 b:23.5 occ:1.00 NE2 A:HIS405 2.0 16.9 1.0 NE2 A:HIS415 2.1 21.4 1.0 O4 A:5411 2.1 25.8 0.8 NE2 A:HIS409 2.1 16.9 1.0 O1 A:5411 2.2 23.1 0.8 C24 A:5411 2.8 25.6 0.8 N2 A:5411 2.9 24.0 0.8 CE1 A:HIS405 3.0 17.2 1.0 CD2 A:HIS405 3.0 16.9 1.0 CE1 A:HIS415 3.0 21.3 1.0 CD2 A:HIS415 3.0 20.6 1.0 CD2 A:HIS409 3.1 16.4 1.0 CE1 A:HIS409 3.2 16.8 1.0 O A:HOH501 3.9 22.0 1.0 ND1 A:HIS405 4.1 17.6 1.0 ND1 A:HIS415 4.1 22.1 1.0 CG A:HIS405 4.1 17.0 1.0 CG A:HIS415 4.2 21.8 1.0 CG A:HIS409 4.3 16.5 1.0 ND1 A:HIS409 4.3 16.9 1.0 C23 A:5411 4.3 26.9 0.8 OE1 A:GLU406 4.6 16.5 1.0 CE A:MET435 4.7 19.5 1.0 N3 A:5411 4.8 27.7 0.8 O A:HOH635 4.8 82.8 1.0 C19 A:5411 4.9 28.2 0.8 OE2 A:GLU406 4.9 16.8 1.0 O A:HOH595 4.9 53.7 1.0 C25 A:5411 5.0 27.4 0.8

Zinc binding site 2 out of 2 in the Crystal Structure of Tace in Complex with IK682


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 IK682 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4 b:24.7 occ:1.00 NE2 B:HIS415 2.1 21.1 1.0 NE2 B:HIS409 2.1 20.7 1.0 O4 B:5412 2.1 25.4 0.9 NE2 B:HIS405 2.2 18.0 1.0 O1 B:5412 2.2 21.7 0.9 C24 B:5412 2.8 24.9 0.9 N2 B:5412 2.9 24.1 0.9 CE1 B:HIS415 3.0 19.8 1.0 CD2 B:HIS405 3.0 18.1 1.0 CD2 B:HIS409 3.0 19.3 1.0 CD2 B:HIS415 3.1 20.3 1.0 CE1 B:HIS409 3.2 19.3 1.0 CE1 B:HIS405 3.2 18.1 1.0 O B:HOH493 4.1 30.3 1.0 ND1 B:HIS415 4.1 20.4 1.0 CG B:HIS405 4.2 17.6 1.0 CG B:HIS415 4.2 20.7 1.0 CG B:HIS409 4.2 20.1 1.0 ND1 B:HIS409 4.2 19.7 1.0 ND1 B:HIS405 4.3 18.4 1.0 C23 B:5412 4.3 25.5 0.9 OE1 B:GLU406 4.6 19.0 1.0 CE B:MET435 4.7 20.5 1.0 N3 B:5412 4.8 26.2 0.9 OE2 B:GLU406 4.9 18.9 1.0 C19 B:5412 5.0 27.0 0.9

X.Niu, S.Umland, R.Ingram, B.M.Beyer, Y.H.Liu, J.Sun, D.Lundell, P.Orth. IK682, A Tight Binding Inhibitor of Tace. Arch.Biochem.Biophys. V. 451 43 2006.
ISSN: ISSN 0003-9861
PubMed: 16762314
DOI: 10.1016/J.ABB.2006.03.034