Zinc in PDB 1biw: Design and Synthesis of Conformationally-Constrained Mmp Inhibitors

All present enzymatic activity of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors:
3.4.24.17;

The structure of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors, PDB code: 1biw was solved by M.G.Natchus, M.Cheng, C.T.Wahl, S.Pikul, N.G.Almstead, R.S.Bradley, Y.O.Taiwo, G.E.Mieling, C.M.Dunaway, C.E.Snider, J.M.Mciver, B.L.Barnett, S.J.Mcphail, M.B.Anastasio, B.De, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.060, 77.280, 106.400, 90.00, 90.00, 90.00
R / Rfree (%)	24.7 / 27.5

The structure of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors also contains other interesting chemical elements:

Calcium

(Ca)

6 atoms

The binding sites of Zinc atom in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors (pdb code 1biw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors, PDB code: 1biw:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:12.3 occ:1.00 NE2 A:HIS201 2.1 1.5 1.0 NE2 A:HIS205 2.2 3.4 1.0 NE2 A:HIS211 2.3 12.9 1.0 CD2 A:HIS201 2.8 1.5 1.0 CD2 A:HIS205 2.9 1.5 1.0 CD2 A:HIS211 3.1 12.6 1.0 CE1 A:HIS211 3.3 8.6 1.0 CE1 A:HIS201 3.4 2.3 1.0 CE1 A:HIS205 3.4 4.2 1.0 CG A:HIS201 4.1 1.5 1.0 CG A:HIS205 4.2 1.5 1.0 CG A:HIS211 4.3 5.6 1.0 OE1 A:GLU202 4.3 12.8 1.0 ND1 A:HIS201 4.3 1.5 1.0 OE2 A:GLU202 4.4 8.4 1.0 ND1 A:HIS205 4.4 1.5 1.0 ND1 A:HIS211 4.5 7.5 1.0 CD A:GLU202 4.7 8.0 1.0 CE A:MET219 5.0 1.5 1.0

Zinc binding site 2 out of 4 in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:9.1 occ:1.00 OD2 A:ASP153 1.9 17.6 1.0 NE2 A:HIS166 2.0 6.5 1.0 NE2 A:HIS151 2.1 2.0 1.0 OD1 A:ASP153 2.3 10.1 1.0 ND1 A:HIS179 2.4 5.5 1.0 CG A:ASP153 2.5 8.0 1.0 CE1 A:HIS166 2.9 6.7 1.0 CD2 A:HIS151 3.0 3.4 1.0 CE1 A:HIS151 3.1 1.5 1.0 CD2 A:HIS166 3.2 6.9 1.0 CE1 A:HIS179 3.3 2.6 1.0 CG A:HIS179 3.4 4.0 1.0 CB A:HIS179 3.8 1.5 1.0 CB A:ASP153 4.0 8.5 1.0 O A:TYR155 4.0 7.9 1.0 ND1 A:HIS166 4.1 6.7 1.0 CG A:HIS151 4.1 6.4 1.0 ND1 A:HIS151 4.2 2.6 1.0 CG A:HIS166 4.3 5.6 1.0 OH A:TYR168 4.3 4.0 1.0 NE2 A:HIS179 4.5 4.1 1.0 CD2 A:HIS179 4.6 1.5 1.0 O A:HOH307 4.6 3.6 1.0 CE1 A:TYR168 4.7 1.5 1.0 CE1 A:PHE157 4.8 1.5 1.0 CB A:TYR155 4.9 6.7 1.0 C A:TYR155 4.9 8.8 1.0 CZ A:PHE157 4.9 1.5 1.0 CA A:ASP153 5.0 12.0 1.0 N A:ASP153 5.0 14.7 1.0

Zinc binding site 3 out of 4 in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn801 b:16.6 occ:1.00 O2 B:S80401 1.9 11.8 1.0 O1 B:S80401 2.1 19.1 1.0 NE2 B:HIS201 2.1 1.5 1.0 NE2 B:HIS205 2.1 1.5 1.0 NE2 B:HIS211 2.2 3.8 1.0 N1 B:S80401 2.8 5.8 1.0 C1 B:S80401 2.8 14.4 1.0 CD2 B:HIS201 2.8 2.3 1.0 CD2 B:HIS205 3.0 1.5 1.0 CD2 B:HIS211 3.1 1.5 1.0 CE1 B:HIS205 3.2 1.5 1.0 CE1 B:HIS211 3.3 1.5 1.0 CE1 B:HIS201 3.4 3.5 1.0 OE2 B:GLU202 3.6 8.8 1.0 CG B:HIS201 4.1 1.5 1.0 C2 B:S80401 4.2 16.4 1.0 CG B:HIS205 4.2 4.1 1.0 CD B:GLU202 4.3 5.0 1.0 OE1 B:GLU202 4.3 5.0 1.0 ND1 B:HIS201 4.3 1.5 1.0 ND1 B:HIS205 4.3 6.2 1.0 CG B:HIS211 4.3 1.5 1.0 ND1 B:HIS211 4.4 1.5 1.0 C14 B:S80401 4.7 12.0 1.0 CE B:MET219 4.8 7.0 1.0 C3 B:S80401 4.8 15.8 1.0 C17 B:S80401 4.9 9.7 1.0

Zinc binding site 4 out of 4 in the Design and Synthesis of Conformationally-Constrained Mmp Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Design and Synthesis of Conformationally-Constrained Mmp Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn802 b:14.2 occ:1.00 OD2 B:ASP153 2.0 15.5 1.0 NE2 B:HIS166 2.0 3.5 1.0 NE2 B:HIS151 2.1 5.1 1.0 ND1 B:HIS179 2.3 8.7 1.0 OD1 B:ASP153 2.5 4.9 1.0 CG B:ASP153 2.6 9.7 1.0 CD2 B:HIS151 2.9 2.3 1.0 CE1 B:HIS166 3.0 7.0 1.0 CE1 B:HIS179 3.1 3.1 1.0 CE1 B:HIS151 3.2 5.6 1.0 CD2 B:HIS166 3.2 2.7 1.0 CG B:HIS179 3.4 4.9 1.0 O B:TYR155 3.7 8.4 1.0 CB B:HIS179 3.9 4.8 1.0 CB B:ASP153 4.0 9.7 1.0 OH B:TYR168 4.1 5.6 1.0 CG B:HIS151 4.1 3.2 1.0 O B:HOH832 4.2 21.2 1.0 ND1 B:HIS151 4.2 2.3 1.0 ND1 B:HIS166 4.2 5.2 1.0 CG B:HIS166 4.3 4.3 1.0 NE2 B:HIS179 4.3 1.5 1.0 CD2 B:HIS179 4.5 5.1 1.0 O B:HOH814 4.7 3.3 1.0 C B:TYR155 4.7 8.8 1.0 CE1 B:PHE157 4.8 11.7 1.0 CE1 B:TYR168 4.8 1.5 1.0 CZ B:TYR168 4.9 3.0 1.0 CZ B:PHE157 4.9 11.5 1.0 N B:ASP153 4.9 8.8 1.0 CA B:ASP153 5.0 9.7 1.0 CB B:TYR155 5.0 4.3 1.0

M.G.Natchus, M.Cheng, C.T.Wahl, S.Pikul, N.G.Almstead, R.S.Bradley, Y.O.Taiwo, G.E.Mieling, C.M.Dunaway, C.E.Snider, J.M.Mciver, B.L.Barnett, S.J.Mcphail, M.B.Anastasio, B.De. Design and Synthesis of Conformationally-Constrained Mmp Inhibitors. Bioorg.Med.Chem.Lett. V. 8 2077 1998.
ISSN: ISSN 0960-894X
PubMed: 9873489
DOI: 10.1016/S0960-894X(98)00370-9