FAIRMol

KB_chagas_112

Pose ID 777 Compound 48 Pose 777

DB Docking_panel_21Docking pose analysis is being read from this database.
Molecular metrics status: done
Cached molecular metrics are available for this pose.
Metrics cached · SASA missing

py3Dmol interaction viewer

Left: interactive complex viewer. Right: clickable PLIP-like interaction summary. Clicking an interaction thickens and highlights it in the 3D view.
Strict H-bonds Permissive H-bonds
Molecular report
Full metrics ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-0.987 kcal/mol/HA) ✓ Good fit quality (FQ -8.85) ✓ Good H-bonds (3 bonds) ✗ Very high strain energy (34.7 kcal/mol) ✗ Geometry warnings ✗ Protein contact clashes ℹ SASA not computed
Score
-23.695
kcal/mol
LE
-0.987
kcal/mol/HA
Fit Quality
-8.85
FQ (Leeson)
HAC
24
heavy atoms
MW
321
Da
LogP
2.17
cLogP
Strain ΔE
34.7 kcal/mol
SASA buried
computing…
Overall: Promising but geometrically suspicious
Binding evidence: strong
Native-like contacts: strong
Ligand efficiency: excellent
Geometry reliability: low
Reason: geometry warning, clashes, protein contact clashes, strain 34.7 kcal/mol

Interaction summary

Collapsible panels
H-bonds 3 Hydrophobic 24 π–π 1 Clashes 3 Severe clashes 0
Final rank3.3069864070798087Score-23.6945
Inter norm-1.07038Intra norm0.0831082
Top1000noExcludedno
Contacts16H-bonds3
Artifact reasongeometry warning; 11 clashes; 3 protein contact clashes; high strain Δ 30.4
ResiduesA:ALA10;A:ASP22;A:GLU31;A:ILE61;A:ILE8;A:LEU68;A:NAP201;A:PHE32;A:PHE35;A:PRO62;A:SER60;A:THR137;A:THR57;A:TYR122;A:VAL116;A:VAL9

Protein summary

200 residues
Protein targetT02Atoms3128
Residues200Chains2
Residue summaryLYS:374; LEU:361; GLU:240; VAL:224; ARG:192; PHE:180; ILE:171; PRO:168; ASN:140; SER:132; TYR:126; GLN:119; ASP:108; MET:102; THR:98; GLY:91

Native ligand reference

★ reference
Interaction fingerprint calculated directly from the uploaded native ligand without docking. Current H-bond mode: strict.
Name5SD8Contacts21
PoseOpen native poseH-bonds5
IFP residuesA:ALA10; A:ASN65; A:ASP22; A:GLN36; A:GLU31; A:GLY117; A:GLY21; A:ILE61; A:ILE8; A:LEU23; A:LEU68; A:NAP201; A:PHE32; A:PHE35; A:PRO62; A:SER60; A:THR137; A:THR57; A:TYR122; A:VAL116; A:VAL9
Current overlap16Native recall0.76
Jaccard0.76RMSD-
H-bond strict2Strict recall0.40
H-bond same residue+role2Role recall0.40
H-bond same residue2Residue recall0.40

Hydrogen bonds

Mode: strict. Count shows atom-level H-bonds; unique residues in summary: 0.

π–π interactions

Native π–π recall is disabled because no explicit native π–π reference was stored.

Hydrophobic contacts

Clashes

All stored poses for this docking hit

PoseFinal rankInter normScoreHBContactsNative overlapNative recallHB role recallRMSDExcluded
576 2.6237375765059507 -0.93282 -24.0238 3 12 0 0.00 0.00 - no Open
778 3.1110261312777627 -0.925631 -21.4293 1 14 11 0.52 0.20 - no Open
460 3.1267889656501793 -0.982777 -23.5247 1 16 0 0.00 0.00 - no Open
777 3.3069864070798087 -1.07038 -23.6945 3 16 16 0.76 0.40 - no Current
578 3.821904492519729 -0.893133 -16.4562 3 14 0 0.00 0.00 - no Open
461 5.730656184982296 -0.836334 -12.5792 2 14 0 0.00 0.00 - yes Open
577 6.796143925751116 -0.837595 -18.8402 4 12 0 0.00 0.00 - yes Open

Molecular metrics

FreeSASA-based burial, strain energy (MMFF94s), ligand efficiency and fit quality for this docking pose.
✓ Metrics available

Scoring & efficiency

Docking score -23.695kcal/mol
Ligand efficiency (LE) -0.9873kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -8.848
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 24HA

Physicochemical properties

Molecular weight 321.4Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.17
Lipinski: ≤ 5
Rotatable bonds 3

Conformational strain (MMFF94s)

Strain energy (ΔE) 34.75kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 43.56kcal/mol
Minimised FF energy 8.81kcal/mol

SASA & burial (FreeSASA)

not yet run
SASA has not been computed yet for this pose. Queue a background recompute to populate FreeSASA burial metrics without blocking the page.