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Chlorine in PDB 8cnh: Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512

Enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512

All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512:
4.6.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512, PDB code: 8cnh was solved by C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.38 / 2.00
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 99.14, 99.14, 99.601, 90, 90, 120
R / Rfree (%) 18.9 / 23.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512 (pdb code 8cnh). 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 Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512, PDB code: 8cnh:

Chlorine binding site 1 out of 1 in 8cnh

Go back to Chlorine Binding Sites List in 8cnh
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Soluble Adenylyl Cyclase (Sac) in Complex with Inhibitor Tdi-10512 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:31.3
occ:1.00
 CL19 A:V6U501 0.0 31.3 1.0
C02 A:V6U501 1.7 28.5 1.0
N01 A:V6U501 2.7 27.6 1.0
C03 A:V6U501 2.7 25.5 1.0
H031 A:V6U501 2.8 30.6 1.0
HE2 A:PHE165 2.9 45.0 1.0
HG22 A:VAL167 2.9 39.9 1.0
HE3 A:LYS95 3.0 48.1 1.0
HA A:LEU166 3.0 38.1 1.0
H A:VAL167 3.1 37.5 1.0
HD2 A:LYS95 3.2 46.4 1.0
HB3 A:LEU94 3.3 33.1 1.0
CE2 A:PHE165 3.4 37.5 1.0
HD13 A:LEU94 3.5 37.4 1.0
HD2 A:PHE165 3.6 44.0 1.0
N A:VAL167 3.7 31.3 1.0
CD2 A:PHE165 3.7 36.7 1.0
CE A:LYS95 3.8 40.1 1.0
HD23 A:LEU102 3.8 36.6 1.0
CA A:LEU166 3.9 31.8 1.0
CD A:LYS95 3.9 38.7 1.0
CG2 A:VAL167 3.9 33.2 1.0
C06 A:V6U501 4.0 27.5 1.0
HB2 A:LYS95 4.0 40.9 1.0
C04 A:V6U501 4.0 26.8 1.0
C A:LEU166 4.0 32.6 1.0
HG13 A:VAL167 4.1 39.4 1.0
HD23 A:LEU166 4.1 40.1 1.0
CB A:LEU94 4.1 27.6 1.0
HB2 A:LEU94 4.1 33.1 1.0
HZ2 A:LYS95 4.2 50.4 1.0
HG3 A:LYS95 4.2 44.6 1.0
O A:PHE165 4.2 29.4 1.0
HG23 A:VAL167 4.2 39.9 1.0
HD12 A:LEU94 4.3 37.4 1.0
CZ A:PHE165 4.3 38.9 1.0
CD1 A:LEU94 4.3 31.2 1.0
HG21 A:VAL167 4.4 39.9 1.0
HZ A:PHE165 4.4 46.7 1.0
CG A:LYS95 4.5 37.2 1.0
N05 A:V6U501 4.5 26.3 1.0
N A:LEU166 4.5 31.2 1.0
NZ A:LYS95 4.5 42.0 1.0
HE2 A:LYS95 4.5 48.1 1.0
C A:PHE165 4.6 30.6 1.0
CD2 A:LEU102 4.7 30.5 1.0
HD3 A:LYS95 4.7 46.4 1.0
CB A:VAL167 4.7 33.0 1.0
CB A:LYS95 4.7 34.0 1.0
CA A:VAL167 4.8 32.7 1.0
CG A:LEU94 4.8 30.1 1.0
CG1 A:VAL167 4.8 32.8 1.0
HZ1 A:LYS95 4.8 50.4 1.0
HD21 A:LEU102 4.8 36.6 1.0
CG A:PHE165 4.9 35.8 1.0
HD22 A:LEU102 4.9 36.6 1.0
HB3 A:LEU166 5.0 39.5 1.0
HD22 A:LEU94 5.0 36.4 1.0
CB A:LEU166 5.0 32.9 1.0
CD2 A:LEU166 5.0 33.4 1.0

Reference:

S.Sun, M.Fushimi, T.Rossetti, N.Kaur, J.Ferreira, M.Miller, J.Quast, J.Van Den Heuvel, C.Steegborn, L.R.Levin, J.Buck, R.W.Myers, S.Kargman, N.Liverton, P.T.Meinke, D.J.Huggins. Scaffold Hopping and Optimization of Small Molecule Soluble Adenyl Cyclase Inhibitors Led By Free Energy Perturbation. J.Chem.Inf.Model. 2023.
ISSN: ESSN 1549-960X
PubMed: 37060320
DOI: 10.1021/ACS.JCIM.2C01577
Page generated: Tue Jul 30 08:04:18 2024

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