Bromine in PDB 1snk: Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde

All present enzymatic activity of Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde:
3.4.22.38;

The structure of Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde, PDB code: 1snk was solved by E.E.Boros, D.N.Deaton, A.M.Hassell, R.B.Mcfadyen, A.B.Miller, L.R.Miller, L.M.Shewchuk, J.B.Thompson, D.H.Willard Jr., L.L.Wright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	62.073, 62.073, 113.378, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 28.6

The binding sites of Bromine atom in the Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde (pdb code 1snk). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde, PDB code: 1snk:

Bromine binding site 1 out of 1 in the Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Cathepsin K Complexed with Carbamate Derivatized Norleucine Aldehyde within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1 b:69.7 occ:1.00 BR2 A:MYE1 0.0 69.7 1.0 C22 A:MYE1 1.9 62.9 1.0 C21 A:MYE1 2.9 62.4 1.0 C24 A:MYE1 2.9 60.8 1.0 O A:GLU59 3.6 36.8 1.0 O A:ASN60 3.7 36.4 1.0 C A:ASN60 3.7 34.2 1.0 CB A:ASP61 3.9 32.8 1.0 CA A:ASN60 4.2 34.4 1.0 N A:ASP61 4.2 32.8 1.0 C20 A:MYE1 4.2 58.9 1.0 C25 A:MYE1 4.2 57.9 1.0 C A:GLU59 4.4 36.4 1.0 CA A:ASP61 4.5 32.1 1.0 C19 A:MYE1 4.7 56.2 1.0 N A:ASN60 4.7 34.8 1.0 CG A:ASP61 4.8 34.0 1.0

E.E.Boros, D.N.Deaton, A.M.Hassell, R.B.Mcfadyen, A.B.Miller, L.R.Miller, M.G.Paulick, L.M.Shewchuk, J.B.Thompson, D.H.Willard Jr., L.L.Wright. Exploration of the P(2)-P(3) Sar of Aldehyde Cathepsin K Inhibitors Bioorg.Med.Chem.Lett. V. 14 3425 2004.
ISSN: ISSN 0960-894X
PubMed: 15177446
DOI: 10.1016/J.BMCL.2004.04.084