Zinc in PDB 1ekb: The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane

All present enzymatic activity of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane:
3.4.21.9;

The structure of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane, PDB code: 1ekb was solved by K.Fuetterer, D.Lu, J.E.Sadler, G.Waksman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.990, 70.650, 85.220, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 26.9

The binding sites of Zinc atom in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane (pdb code 1ekb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane, PDB code: 1ekb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn310 b:25.5 occ:1.00 OE2 B:GLU126 2.4 22.9 1.0 OE1 B:GLU126 2.7 27.3 1.0 CD B:GLU126 2.9 27.2 1.0 OE1 B:GLU236 4.1 43.7 1.0 CG B:GLU126 4.4 27.3 1.0 CG B:GLU236 4.5 40.1 1.0 CD B:GLU236 4.7 41.5 1.0 CB B:GLU236 4.7 34.7 1.0

Zinc binding site 2 out of 2 in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn311 b:44.7 occ:1.00 OD2 B:ASP50 2.6 31.8 1.0 O B:HOH479 2.7 27.5 1.0 O B:HIS243 2.7 35.4 1.0 CG B:ASP50 3.0 31.4 1.0 C B:HIS243 3.3 39.0 1.0 CB B:ASP50 3.4 26.7 1.0 CA B:HIS243 3.6 39.0 1.0 OD1 B:ASP50 3.9 34.0 1.0 NE2 B:HIS107 4.0 4.2 1.0 N B:HIS243 4.5 39.2 1.0 CD2 B:HIS107 4.6 2.0 1.0 CB B:HIS243 4.7 41.1 1.0 NE1 B:TRP51 4.7 11.3 1.0 CE B:LYS111 4.8 26.6 1.0 CA B:ASP50 4.9 22.8 1.0 O B:HOH456 4.9 19.2 1.0 CD2 B:HIS243 5.0 45.6 1.0

D.Lu, K.Futterer, S.Korolev, X.Zheng, K.Tan, G.Waksman, J.E.Sadler. Crystal Structure of Enteropeptidase Light Chain Complexed with An Analog of the Trypsinogen Activation Peptide. J.Mol.Biol. V. 292 361 1999.
ISSN: ISSN 0022-2836
PubMed: 10493881
DOI: 10.1006/JMBI.1999.3089