Zinc in PDB 3s0n: Crystal Structure of Human Chymase with Benzimidazolone Inhibitor

All present enzymatic activity of Crystal Structure of Human Chymase with Benzimidazolone Inhibitor:
3.4.21.39;

The structure of Crystal Structure of Human Chymase with Benzimidazolone Inhibitor, PDB code: 3s0n was solved by K.C.Qian, N.A.Farrow, A.K.Padyana, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.63 / 1.95
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	73.830, 73.830, 48.450, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Crystal Structure of Human Chymase with Benzimidazolone Inhibitor (pdb code 3s0n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Chymase with Benzimidazolone Inhibitor, PDB code: 3s0n:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Chymase with Benzimidazolone Inhibitor


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 Human Chymase with Benzimidazolone Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn229 b:22.7 occ:1.00 OE1 A:GLU64 1.9 26.8 1.0 NE2 A:HIS10 2.1 19.2 1.0 CD A:GLU64 2.7 25.0 1.0 OE2 A:GLU64 2.9 24.2 1.0 CE1 A:HIS10 3.0 18.0 1.0 CD2 A:HIS10 3.1 17.8 1.0 OG1 A:THR66 3.8 19.1 1.0 CG2 A:THR66 4.1 19.2 1.0 CG A:GLU64 4.1 25.5 1.0 ND1 A:HIS10 4.1 18.1 1.0 CG A:HIS10 4.2 17.4 1.0 O A:HOH324 4.3 27.4 1.0 CB A:THR66 4.6 19.6 1.0 CB A:GLU64 4.7 23.6 1.0

H.Y.Lo, P.A.Nemoto, J.M.Kim, M.H.Hao, K.C.Qian, N.A.Farrow, D.R.Albaugh, D.M.Fowler, R.D.Schneiderman, E.Michael August, L.Martin, M.Hill-Drzewi, S.S.Pullen, H.Takahashi, S.De Lombaert. Benzimidazolone As Potent Chymase Inhibitor: Modulation of Reactive Metabolite Formation in the Hydrophobic (P(1)) Region. Bioorg.Med.Chem.Lett. V. 21 4533 2011.
ISSN: ISSN 0960-894X
PubMed: 21733690
DOI: 10.1016/J.BMCL.2011.05.126