Chlorine in PDB 4gqq: Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate

All present enzymatic activity of Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate:
3.2.1.1;

The structure of Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate, PDB code: 4gqq was solved by L.K.Williams, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.06 / 1.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.060, 68.120, 125.910, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.7

The structure of Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate (pdb code 4gqq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate, PDB code: 4gqq:

Chlorine binding site 1 out of 1 in the Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Pancreatic Alpha-Amylase with Bound Ethyl Caffeate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:24.1 occ:0.50 NE A:ARG195 3.0 14.3 1.0 NH2 A:ARG195 3.3 15.1 1.0 NH1 A:ARG337 3.4 15.8 1.0 NH2 A:ARG337 3.4 17.6 1.0 CG2 A:THR254 3.5 10.0 1.0 CG A:GLU233 3.5 16.1 1.0 CZ A:ARG195 3.5 13.1 1.0 CZ A:ARG337 3.9 15.6 1.0 CB A:GLU233 4.0 10.8 1.0 CD A:ARG195 4.0 13.0 1.0 CZ A:PHE256 4.3 14.4 1.0 CG A:ARG195 4.4 11.2 1.0 CD A:GLU233 4.4 18.9 1.0 OE1 A:GLU233 4.5 23.3 1.0 CE2 A:PHE256 4.6 13.1 1.0 CB A:THR254 4.6 10.1 1.0 CA A:GLU233 4.7 9.0 1.0 NH1 A:ARG195 4.9 12.8 1.0 CZ A:PHE295 4.9 13.5 1.0 OG1 A:THR254 5.0 10.3 1.0

L.K.Williams, C.Li, S.G.Withers, G.D.Brayer. Order and Disorder: Differential Structural Impacts of Myricetin and Ethyl Caffeate on Human Amylase, An Antidiabetic Target. J.Med.Chem. V. 55 10177 2012.
ISSN: ISSN 0022-2623
PubMed: 23050660
DOI: 10.1021/JM301273U