FAIRMol

KB_chagas_179

Pose ID 9632 Compound 2496 Pose 146

DB fairmolDocking pose analysis is being read from this database.
Compound detail Protein structures Back to compounds
Molecular metrics status: done
RDKit SASA-based burial metrics are cached.
SASA cached
T15
T. brucei TR (Dimer cleft site) T. brucei Dimer cleft site
Ligand KB_chagas_179
PDB9IFF↗

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Weak SASA cached
Promising but geometrically suspicious
Binding strong Geometry low Native strong SASA done
Strain ΔE
12.9 kcal/mol
Protein clashes
0
Internal clashes
11
Native overlap
contact recall 0.69, Jaccard 0.45
Burial
76%
Hydrophobic fit
91%
Reason: 11 internal clashes
11 intramolecular clashes
Molecular report
Full metrics ↗
Weak Marginal quality. Consider only alongside better-scoring alternatives.
✓ Excellent LE (-0.872 kcal/mol/HA) ✓ Good fit quality (FQ -8.03) ✓ Good H-bonds (4 bonds) ✓ Deep burial (76% SASA buried) ✓ Lipophilic contacts well-matched (91%) ✗ Moderate strain (12.9 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (11)
Score
-22.664
kcal/mol
LE
-0.872
kcal/mol/HA
Fit Quality
-8.03
FQ (Leeson)
HAC
26
heavy atoms
MW
351
Da
LogP
2.96
cLogP
Final rank
2.0844
rank score
Inter norm
-0.923
normalised
Contacts
16
H-bonds 5
Strain ΔE
12.9 kcal/mol
SASA buried
76%
Lipo contact
91% BSA apolar/total
SASA unbound
621 Ų
Apolar buried
427 Ų

Interaction summary

HBD 3 HBA 1 HY 9 PI 0 CLASH 0

HBD/HBA · H-bonds (geometric)
HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: strict. Residues: 3.

PI · π–π interactions
No pi · π–π interactions detected for this pose.

HY · Hydrophobic contacts

CLASH · Clashes
No clash · clashes detected for this pose.

Native ligand reference

★ reference
Interaction fingerprint calculated directly from the uploaded native ligand without docking. Current H-bond mode: strict.
Name9IFFContacts13
PoseOpen native poseHB0
IFP residues
ALA209 ARG74 ASN208 GLY214 GLY215 GLY85 LEU73 LYS211 MET70 PHE83 PRO212 PRO213 VAL88
Current overlap9Native recall0.69
Jaccard0.45RMSD-
HB strict0Strict recall-
HB same residue+role0HB role recall-
HB same residue0HB residue recall-

Protein summary

489 residues
Protein targetT15Atoms7420
Residues489Chains1
Residue summaryVAL:768; LYS:704; LEU:703; ILE:532; GLU:450; THR:434; ARG:408; PHE:400; ALA:390; ASN:350; PRO:350; GLY:336; SER:319; TYR:294; ASP:264; MET:204

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
159 1.1455860854604214 -1.08924 -20.3378 5 19 0 0.00 - - no Open
146 2.084418835593958 -0.922979 -22.6636 5 16 9 0.69 - - no Current
145 2.2292695857404397 -0.936955 -16.5494 3 15 0 0.00 - - no Open
178 2.3134423439271834 -1.25978 -27.7542 4 17 0 0.00 - - no Open
134 2.9966302811408103 -0.983186 -24.2761 8 14 0 0.00 - - no Open
188 4.357865830563273 -0.8234 -10.1582 6 11 0 0.00 - - no Open
168 4.8756264276749945 -0.823257 -22.1552 7 13 0 0.00 - - no Open

Molecular metrics

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

Scoring & efficiency
Docking score -22.664kcal/mol
Ligand efficiency (LE) -0.8717kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -8.031
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 26HA

Physicochemical properties
Molecular weight 351.4Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.96
Lipinski: ≤ 5
Rotatable bonds 5

Conformational strain (MMFF94s)
Strain energy (ΔE) 12.91kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy -22.60kcal/mol
Minimised FF energy -35.51kcal/mol

SASA & burial

✓ computed
SASA (unbound) 620.8Ų
Total solvent-accessible surface area of free ligand
BSA total 470.2Ų
Buried surface area upon binding
BSA apolar 427.1Ų
Hydrophobic contacts buried
BSA polar 43.0Ų
Polar contacts buried
Fraction buried 75.7%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 90.8%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -3020.6Ų
SASA_nonpolar(complex) − SASA_nonpolar(receptor) − SASA_nonpolar(ligand free). Negative = non-polar surface buried upon binding. Requires full polarity-decomposed SASA computation.
Receptor non-polar SASA 4005.2Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 1554.3Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)