Chlorine in PDB 4oyo: Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole

All present enzymatic activity of Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole:
4.6.1.1;

The structure of Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole, PDB code: 4oyo was solved by M.Vinkovic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.88 / 1.75
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	100.031, 100.031, 98.011, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 21.2

The binding sites of Chlorine atom in the Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole (pdb code 4oyo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole, PDB code: 4oyo:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole


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 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:40.0 occ:0.50 CL1 A:1WC501 0.0 40.0 0.5 C13 A:1WC501 1.7 39.2 0.5 C12 A:1WC501 2.7 40.2 0.5 C8 A:1WC501 2.7 36.4 0.5 H22 A:1WC501 2.8 40.4 0.5 H20 A:1WC502 2.8 30.2 1.0 H18 A:1WC501 2.8 31.0 0.5 C7 A:1WC501 3.1 32.1 0.5 C6 A:1WC501 3.1 30.5 0.5 C10 A:1WC502 3.7 29.9 1.0 H22 A:1WC503 3.7 35.3 1.0 CB A:ALA97 3.8 20.3 1.0 C12 A:1WC503 3.9 34.3 1.0 O A:ALA97 3.9 26.4 1.0 C11 A:1WC501 4.0 39.7 0.5 C9 A:1WC501 4.0 39.3 0.5 H21 A:1WC502 4.1 28.8 1.0 N5 A:1WC501 4.2 28.7 0.5 C2 A:1WC501 4.3 30.4 0.5 C11 A:1WC502 4.3 28.0 1.0 C13 A:1WC503 4.3 33.3 1.0 CZ A:PHE45 4.3 34.3 1.0 C11 A:1WC503 4.3 32.3 1.0 C A:ALA97 4.4 27.8 1.0 H21 A:1WC503 4.4 31.9 1.0 C10 A:1WC501 4.5 40.0 0.5 H19 A:1WC502 4.6 29.5 1.0 CL1 A:1WC503 4.6 36.8 1.0 CB A:ALA100 4.6 22.5 1.0 C9 A:1WC502 4.6 27.9 1.0 H21 A:1WC501 4.7 39.6 0.5 CA A:ALA97 4.7 19.4 1.0 H19 A:1WC501 4.8 39.4 0.5 N3 A:1WC501 4.8 28.7 0.5 CZ A:PHE336 4.8 26.0 1.0 CE1 A:PHE45 4.8 33.9 1.0 CE2 A:PHE336 4.9 26.1 1.0 CE1 A:PHE336 5.0 27.3 1.0

Chlorine binding site 2 out of 3 in the Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:38.2 occ:1.00 CL1 A:1WC502 0.0 38.2 1.0 C13 A:1WC502 1.7 31.5 1.0 H17 A:1WC502 2.5 26.4 1.0 H15 A:1WC502 2.6 22.2 1.0 C12 A:1WC502 2.7 31.2 1.0 C8 A:1WC502 2.7 26.6 1.0 H22 A:1WC502 2.8 31.8 1.0 C1 A:1WC502 2.9 24.1 1.0 CD2 A:LEU102 3.1 21.2 1.0 C7 A:1WC502 3.2 27.8 1.0 CB A:LYS95 3.2 18.6 1.0 C2 A:1WC502 3.2 26.1 1.0 CB A:LEU102 3.6 11.0 1.0 CB A:LEU94 3.6 9.4 1.0 H16 A:1WC502 3.8 27.1 1.0 CG A:LEU102 3.9 17.3 1.0 C11 A:1WC502 4.0 28.0 1.0 N A:LYS95 4.0 9.4 1.0 C9 A:1WC502 4.0 27.9 1.0 CD A:LYS95 4.1 34.5 1.0 CA A:LYS95 4.2 10.9 1.0 CG A:LYS95 4.3 33.0 1.0 C A:LEU94 4.3 11.2 1.0 C6 A:1WC502 4.4 29.1 1.0 CD1 A:LEU94 4.4 12.4 1.0 N3 A:1WC502 4.4 26.4 1.0 C10 A:1WC502 4.5 29.9 1.0 CE A:LYS95 4.5 29.1 1.0 CA A:LEU94 4.6 6.9 1.0 CG A:LEU94 4.7 11.3 1.0 H21 A:1WC502 4.7 28.8 1.0 CG2 A:VAL167 4.7 15.2 1.0 H19 A:1WC502 4.7 29.5 1.0 O A:LYS95 4.8 12.6 1.0 O A:LEU94 4.8 10.3 1.0 O A:LEU102 4.9 11.7 1.0 C A:LYS95 4.9 12.2 1.0 CA A:LEU102 4.9 9.9 1.0 N5 A:1WC502 5.0 23.4 1.0 H18 A:1WC502 5.0 28.1 1.0

Chlorine binding site 3 out of 3 in the Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Human Solac Complexed with 4-(2-Chlorophenyl)-3-Methyl-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:36.8 occ:1.00 CL1 A:1WC503 0.0 36.8 1.0 C13 A:1WC503 1.7 33.3 1.0 C12 A:1WC503 2.7 34.3 1.0 C8 A:1WC503 2.7 31.6 1.0 H22 A:1WC503 2.8 35.3 1.0 H18 A:1WC503 2.8 34.2 1.0 C7 A:1WC503 3.2 32.0 1.0 C6 A:1WC503 3.2 33.0 1.0 N A:GLY98 3.5 25.9 1.0 CA A:GLY98 3.6 27.2 1.0 H18 A:1WC501 3.8 31.0 0.5 CD1 A:LEU345 3.9 17.6 1.0 C11 A:1WC503 4.0 32.3 1.0 O A:HOH1116 4.0 33.7 1.0 C9 A:1WC503 4.0 32.7 1.0 C A:ALA97 4.2 27.8 1.0 CG1 A:VAL411 4.2 16.8 1.0 N5 A:1WC503 4.3 33.3 1.0 C2 A:1WC503 4.4 34.4 1.0 CE2 A:PHE296 4.5 15.8 1.0 CB A:ALA97 4.5 20.3 1.0 CZ A:PHE296 4.5 13.9 1.0 C10 A:1WC503 4.5 33.1 1.0 CL1 A:1WC501 4.6 40.0 0.5 H21 A:1WC503 4.7 31.9 1.0 CA A:ALA97 4.7 19.4 1.0 C6 A:1WC501 4.8 30.5 0.5 H19 A:1WC503 4.8 31.5 1.0 O A:ALA97 4.8 26.4 1.0 CE2 A:PHE336 4.9 26.1 1.0 O A:VAL406 4.9 20.0 1.0 N3 A:1WC503 4.9 35.3 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