FAIRMol

Z49643066

Pose ID 10061 Compound 942 Pose 575

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 Z49643066
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
Promising but geometrically suspicious
Binding strong Geometry low Native strong SASA done
Strain ΔE
57.9 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.62, Jaccard 0.38
Burial
64%
Hydrophobic fit
80%
Reason: strain 57.9 kcal/mol
strain ΔE 57.9 kcal/mol 2 protein-contact clashes 61% of hydrophobic surface is solvent-exposed (17/28 atoms). Large non-polar area without protein contacts incurs a desolvation penalty and will reduce binding affinity. Consider truncating or replacing the exposed fragment.
Molecular report
Full metrics ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-0.527 kcal/mol/HA) ✓ Good fit quality (FQ -5.54) ✓ Good H-bonds (4 bonds) ✓ Good burial (64% SASA buried) ✓ Lipophilic contacts well-matched (80%) ✗ Extreme strain energy (57.9 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (16)
Score
-21.614
kcal/mol
LE
-0.527
kcal/mol/HA
Fit Quality
-5.54
FQ (Leeson)
HAC
41
heavy atoms
MW
594
Da
LogP
5.31
cLogP
Final rank
3.7318
rank score
Inter norm
-0.643
normalised
Contacts
16
H-bonds 5
Strain ΔE
57.9 kcal/mol
SASA buried
64%
Lipo contact
80% BSA apolar/total
SASA unbound
916 Ų
Apolar buried
472 Ų

Interaction summary

HBD 1 HBA 3 HY 7 PI 0 CLASH 2

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 overlap8Native recall0.62
Jaccard0.38RMSD-
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
557 2.4874861206743537 -0.648148 -20.6373 4 18 0 0.00 - - no Open
524 3.2596614552604413 -0.532423 -19.7552 5 10 0 0.00 - - no Open
556 3.340626388392719 -0.596833 -21.321 4 19 0 0.00 - - no Open
575 3.7317739710158384 -0.642522 -21.6137 5 16 8 0.62 - - 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 -21.614kcal/mol
Ligand efficiency (LE) -0.5272kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -5.539
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 41HA

Physicochemical properties

Molecular weight 593.7Da
Lipinski: ≤ 500 Da
LogP (cLogP) 5.31
Lipinski: ≤ 5
Rotatable bonds 9

Conformational strain (MMFF94s)

Strain energy (ΔE) 57.92kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 82.44kcal/mol
Minimised FF energy 24.52kcal/mol

SASA & burial

✓ computed
SASA (unbound) 915.5Ų
Total solvent-accessible surface area of free ligand
BSA total 586.1Ų
Buried surface area upon binding
BSA apolar 472.0Ų
Hydrophobic contacts buried
BSA polar 114.1Ų
Polar contacts buried
Fraction buried 64.0%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 80.5%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -3186.4Ų
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 1541.4Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)