Zinc in PDB 1c2k: Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases

All present enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases:
3.4.21.4;

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2k was solved by B.A.Katz, C.Luong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.50 / 1.65
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	54.910, 54.910, 108.930, 90.00, 90.00, 120.00
R / Rfree (%)	20.2 / 24.3

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Zinc atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases (pdb code 1c2k). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2k:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn258 b:37.7 occ:0.51 OG A:SER195 2.1 31.1 1.0 N3 A:ABI246 2.4 53.5 0.7 NE2 A:HIS57 2.8 42.3 1.0 C8 A:ABI246 3.2 55.8 0.7 CB A:SER195 3.2 24.5 1.0 HC8 A:ABI246 3.2 55.8 0.7 HB3 A:SER195 3.3 25.7 1.0 CD2 A:HIS57 3.5 42.9 1.0 C4 A:ABI246 3.5 53.0 0.7 HD2 A:HIS57 3.6 41.0 1.0 CE1 A:HIS57 3.7 40.7 1.0 HB2 A:SER195 3.7 26.4 1.0 HC3 A:ABI246 3.7 50.8 0.7 HE1 A:HIS57 3.9 39.5 1.0 C3 A:ABI246 4.0 50.4 0.7 O A:SER214 4.2 10.8 1.0 HA A:GLN192 4.2 37.6 1.0 H A:GLY193 4.3 35.5 1.0 CA A:SER195 4.4 25.2 1.0 N4 A:ABI246 4.4 55.4 0.7 HG3 A:GLN192 4.4 35.6 0.3 H A:SER195 4.5 28.3 1.0 HA A:SER195 4.5 24.5 1.0 C5 A:ABI246 4.6 54.2 0.7 CG A:HIS57 4.6 37.8 1.0 ND1 A:HIS57 4.6 39.9 1.0 N A:SER195 4.9 30.6 1.0 HA A:TRP215 4.9 16.2 1.0

Zinc binding site 2 out of 2 in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn261 b:41.5 occ:0.92 O A:GLY193 2.1 43.5 1.0 CL A:CL250 2.3 31.3 0.8 C A:GLY193 2.3 36.9 1.0 NE2 A:HIS40 2.4 14.8 1.0 HA A:ASP194 2.9 32.7 1.0 N A:ASP194 3.0 34.2 1.0 CA A:GLY193 3.0 36.9 1.0 HA3 A:GLY193 3.0 35.7 1.0 HA2 A:GLY193 3.1 35.8 1.0 H A:TRP141 3.2 23.3 1.0 CD2 A:HIS40 3.4 11.4 1.0 CE1 A:HIS40 3.4 13.2 1.0 CA A:ASP194 3.5 32.5 1.0 HD2 A:HIS40 3.5 11.2 1.0 HA A:CYS42 3.6 10.8 1.0 HE1 A:HIS40 3.6 14.5 1.0 HB2 A:TRP141 3.6 22.4 1.0 HA2 A:GLY142 3.6 35.2 1.0 H A:ASP194 3.7 33.4 1.0 N A:GLY142 3.7 28.8 1.0 H A:GLY142 3.9 30.1 1.0 C A:TRP141 3.9 27.3 1.0 HA3 A:GLY142 4.0 34.9 1.0 HE3 A:TRP141 4.0 16.6 1.0 CA A:GLY142 4.0 34.9 1.0 N A:TRP141 4.0 25.2 1.0 C A:ASP194 4.3 30.8 1.0 H1 A:HOH263 4.3 29.2 1.0 H A:SER195 4.3 28.3 1.0 C A:CYS42 4.3 12.7 1.0 CA A:CYS42 4.3 11.1 1.0 O A:TRP141 4.3 30.2 1.0 N A:GLY193 4.4 35.5 1.0 CA A:TRP141 4.4 25.0 1.0 N A:GLY43 4.4 7.6 1.0 H A:GLY43 4.5 9.6 1.0 CB A:TRP141 4.5 22.1 1.0 OD2 A:ASP194 4.5 32.8 1.0 ND1 A:HIS40 4.5 15.6 1.0 CG A:HIS40 4.6 11.4 1.0 N A:SER195 4.6 30.6 1.0 N A:CYS42 4.6 12.6 1.0 O A:PHE41 4.7 17.6 1.0 O A:CYS42 4.7 12.8 1.0 CB A:ASP194 4.8 32.6 1.0 HA3 A:GLY43 4.8 10.6 1.0 HA3 A:GLY140 4.8 22.4 1.0 C A:PHE41 4.8 12.6 1.0 H A:GLY193 4.9 35.5 1.0 CG A:ASP194 4.9 30.8 1.0 HB3 A:TRP141 5.0 22.4 1.0 O A:HOH263 5.0 32.1 1.0

B.A.Katz, J.M.Clark, J.S.Finer-Moore, T.E.Jenkins, C.R.Johnson, M.J.Ross, C.Luong, W.R.Moore, R.M.Stroud. Design of Potent Selective Zinc-Mediated Serine Protease Inhibitors. Nature V. 391 608 1998.
ISSN: ISSN 0028-0836
PubMed: 9468142
DOI: 10.1038/35422