Ligand profile

HX5

Ligand co-crystallized with a similar protein (Protein Data Bank).

Bound to: KP13_00051 — DNA gyrase subunit B

Via homolog PDB 5z9n UniProt P0AES6 Formula C₅H₄Cl₂N₂S
Mol. weight 195.07 Da
Permeability High
PAINS Clean

Identifiers

Database identifiers and provenance.

Ligand ID
HX5
PDB
5z9n
UniProt (similar protein)
P0AES6
Target protein
KP13_00051

Structure

2D representation rendered from SMILES.

Physicochemical properties

Computed with RDKit from SMILES.

Molecular weight 195.07 Da
LogP (Crippen) 2.51
H-bond donors 0
H-bond acceptors 3
TPSA 25.78 Ų
Rotatable bonds 1
Aromatic rings 1 / 1
Heavy atoms 10
Fraction sp³ C 0.20
Formula C₅H₄Cl₂N₂S

Drug-likeness

Descriptor-based ADME screening flags from SMILES. These are not experimental toxicity results.

Permeability proxy High

Estimated from TPSA and LogP only: TPSA ≤ 90 Ų and −1 ≤ LogP ≤ 5 are treated as a favorable small-molecule permeability screen.

  • TPSA ≤ 90 Ų 25.8
  • −1 ≤ LogP ≤ 5 2.51
Lipinski's Rule of Five Pass 0 violations
  • MW ≤ 500 Da 195.1
  • LogP ≤ 5 2.51
  • H-bond donors ≤ 5 0
  • H-bond acceptors ≤ 10 3
Veber's rules Pass
  • Rotatable bonds ≤ 10 1
  • TPSA ≤ 140 Ų 25.8
PAINS Clean

No PAINS structural alerts detected.

Chemical representations

Canonical representations for cheminformatics workflows.

SMILES 
CSc1nc(cc(n1)Cl)Cl
InChI 
InChI=1S/C5H4Cl2N2S/c1-10-5-8-3(6)2-4(7)9-5/h2H,1H3
InChIKey 
FCMLONIWOAGZJX-UHFFFAOYSA-N

Provenance

Annotation context from LigQ_2, the internal Target step that collects PDB, ChEMBL, and ZINC ligand evidence.

Method
LigQ sequence
Source
PDB
Binding sites
PF02518

External resources

Open this ligand in third-party databases and cheminformatics tools.

Other ligands for this protein

Quick navigation to other ligands bound to KP13_00051.

PDB 87

Ligands co-crystallized with this protein (structural evidence).

Ligand PDB entry

ChEMBL 100

Compounds with measured inhibitory activity on this target (higher pchembl = more potent).

Compound Potency (pchembl)

ZINC 50

Virtual screening candidates selected by structural similarity to known actives (Tanimoto ≥ 0.5).

Compound Similarity (Tanimoto)