FAIRMol

OSA_Lib_65

Pose ID 9665 Compound 4274 Pose 179

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 OSA_Lib_65
PDB9IFF↗

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Reject SASA cached
Likely artefact or unreliable pose
Binding strong Geometry medium Native strong SASA done
Strain ΔE
22.8 kcal/mol
Protein clashes
3
Internal clashes
3
Native overlap
contact recall 0.69, Jaccard 0.50
Burial
69%
Hydrophobic fit
100%
Reason: no major geometry red flags detected
3 protein-contact clashes 3 intramolecular clashes 38% of hydrophobic surface appears solvent-exposed (9/24 atoms). Partial exposure is common but may limit selectivity and membrane permeability.
Molecular report
Full metrics ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-0.814 kcal/mol/HA) ✓ Good fit quality (FQ -7.77) ✓ Good H-bonds (3 bonds) ✓ Deep burial (69% SASA buried) ✓ Lipophilic contacts well-matched (100%) ✗ High strain energy (22.8 kcal/mol) ✗ Geometry warnings ✗ Protein-contact clashes (6) ✗ Many internal clashes (10)
Score
-23.609
kcal/mol
LE
-0.814
kcal/mol/HA
Fit Quality
-7.77
FQ (Leeson)
HAC
29
heavy atoms
MW
434
Da
LogP
2.85
cLogP
Final rank
1.2050
rank score
Inter norm
-0.893
normalised
Contacts
14
H-bonds 4
Strain ΔE
22.8 kcal/mol
SASA buried
69%
Lipo contact
100% BSA apolar/total
SASA unbound
660 Ų
Apolar buried
454 Ų

Interaction summary

HBD 3 HY 8 PI 0 CLASH 3

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

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
Jaccard0.50RMSD-
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
179 1.2049693667942007 -0.892831 -23.6087 4 14 9 0.69 - - no Current
171 3.616169993250942 -0.806551 -22.2188 3 17 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 -23.609kcal/mol
Ligand efficiency (LE) -0.8141kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -7.771
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 29HA

Physicochemical properties
Molecular weight 434.5Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.85
Lipinski: ≤ 5
Rotatable bonds 6

Conformational strain (MMFF94s)
Strain energy (ΔE) 22.82kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 161.58kcal/mol
Minimised FF energy 138.76kcal/mol

SASA & burial

✓ computed
SASA (unbound) 659.9Ų
Total solvent-accessible surface area of free ligand
BSA total 455.7Ų
Buried surface area upon binding
BSA apolar 454.5Ų
Hydrophobic contacts buried
BSA polar 1.2Ų
Polar contacts buried
Fraction buried 69.1%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 99.7%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -3093.3Ų
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 1569.9Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)