FAIRMol

OHD_MAC_48

Pose ID 9959 Compound 900 Pose 473

DB fairmolDocking pose analysis is being read from this database.
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 OHD_MAC_48
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
Weak or marginal quality
Binding strong Geometry medium Native strong SASA done
Strain ΔE
38.7 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.85, Jaccard 0.65
Burial
71%
Hydrophobic fit
79%
Reason: no major geometry red flags detected
2 protein-contact clashes
Molecular report
Full metrics ↗
Weak Marginal quality. Consider only alongside better-scoring alternatives.
✓ Excellent LE (-0.644 kcal/mol/HA) ✓ Good fit quality (FQ -6.44) ✓ Good H-bonds (5 bonds) ✓ Deep burial (71% SASA buried) ✓ Lipophilic contacts well-matched (79%) ✗ Very high strain energy (38.7 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (16)
Score
-21.887
kcal/mol
LE
-0.644
kcal/mol/HA
Fit Quality
-6.44
FQ (Leeson)
HAC
34
heavy atoms
MW
461
Da
LogP
3.08
cLogP
Final rank
4.9371
rank score
Inter norm
-0.777
normalised
Contacts
15
H-bonds 8
Strain ΔE
38.7 kcal/mol
SASA buried
71%
Lipo contact
79% BSA apolar/total
SASA unbound
793 Ų
Apolar buried
444 Ų

Interaction summary

HBD 3 HBA 2 HY 7 PI 1 CLASH 2

HBD/HBA · H-bonds (geometric)

HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: strict. Residues: 5.

PI · π–π interactions

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

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 overlap11Native recall0.85
Jaccard0.65RMSD-
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
379 1.7515119447063427 -0.628624 -16.1568 7 18 0 0.00 - - no Open
428 2.1508479025996894 -0.801565 -19.3286 5 18 0 0.00 - - no Open
368 3.090122770978229 -0.741059 -15.222 13 13 0 0.00 - - no Open
448 3.187813687353957 -0.756461 -24.6559 5 15 0 0.00 - - no Open
373 3.331493017527665 -0.760459 -20.8381 6 17 0 0.00 - - no Open
338 4.6424814593420125 -0.949318 -28.0247 14 23 0 0.00 - - no Open
473 4.937071202872829 -0.776684 -21.8871 8 15 11 0.85 - - no Current

Molecular metrics

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

Scoring & efficiency

Docking score -21.887kcal/mol
Ligand efficiency (LE) -0.6437kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -6.441
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 34HA

Physicochemical properties

Molecular weight 461.5Da
Lipinski: ≤ 500 Da
LogP (cLogP) 3.08
Lipinski: ≤ 5
Rotatable bonds 12

Conformational strain (MMFF94s)

Strain energy (ΔE) 38.68kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 120.00kcal/mol
Minimised FF energy 81.31kcal/mol

SASA & burial

✓ computed
SASA (unbound) 793.5Ų
Total solvent-accessible surface area of free ligand
BSA total 561.9Ų
Buried surface area upon binding
BSA apolar 444.4Ų
Hydrophobic contacts buried
BSA polar 117.5Ų
Polar contacts buried
Fraction buried 70.8%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 79.1%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -3111.4Ų
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 1544.2Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)