Chlorine in PDB 4oyx: Human Solac Complexed with Ampcpp

All present enzymatic activity of Human Solac Complexed with Ampcpp:
4.6.1.1;

The structure of Human Solac Complexed with Ampcpp, PDB code: 4oyx was solved by M.Vinkovic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.39 / 1.89
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	99.651, 99.651, 96.522, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 23

The structure of Human Solac Complexed with Ampcpp also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Human Solac Complexed with Ampcpp (pdb code 4oyx). 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 Solac Complexed with Ampcpp, PDB code: 4oyx:

Chlorine binding site 1 out of 1 in the Human Solac Complexed with Ampcpp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Solac Complexed with Ampcpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:40.2 occ:1.00 NZ A:LYS95 2.9 21.3 1.0 O A:HOH838 3.0 41.7 1.0 N A:VAL167 3.3 28.2 1.0 CG2 A:VAL167 3.7 31.3 1.0 O A:HOH825 3.7 42.5 1.0 CE A:LYS95 3.8 34.7 1.0 CD A:LYS95 3.8 44.8 1.0 CA A:LEU166 3.9 29.4 1.0 C A:LEU166 4.0 31.2 1.0 CA A:VAL167 4.3 30.4 1.0 CD2 A:LEU102 4.4 24.9 1.0 CB A:VAL167 4.5 33.2 1.0 CE1 A:PHE165 4.5 19.7 1.0 O A:PHE165 4.5 22.6 1.0 O A:VAL167 4.6 31.6 1.0 CD2 A:LEU166 4.7 43.2 1.0 CB A:PHE336 4.7 44.4 1.0 O A:VAL335 4.7 38.3 1.0 CB A:LYS95 4.8 29.0 1.0 CA A:PHE336 4.8 42.2 1.0 N A:LEU166 4.9 26.6 1.0 CB A:LEU166 4.9 32.0 1.0 CD1 A:PHE165 4.9 20.2 1.0 CG A:LYS95 4.9 37.9 1.0 CG1 A:VAL167 4.9 31.6 1.0 C A:VAL167 5.0 36.0 1.0

S.M.Saalau-Bethell, V.Berdini, A.Cleasby, M.Congreve, J.E.Coyle, V.Lock, C.W.Murray, M.A.O'brien, S.J.Rich, T.Sambrook, M.Vinkovic, J.R.Yon, H.Jhoti. Crystal Structure of Human Soluble Adenylate Cyclase Reveals A Distinct, Highly Flexible Allosteric Bicarbonate Binding Pocket. Chemmedchem V. 9 823 2014.
ISSN: ESSN 1860-7187
PubMed: 24616449
DOI: 10.1002/CMDC.201300480