FAIRMol

KB_Leish_137

Pose ID 6898 Compound 3547 Pose 124

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
T11
L. infantum SIR2 L. infantum
Ligand KB_Leish_137

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
29.2 kcal/mol
Protein clashes
3
Internal clashes
3
Native overlap
contact recall 0.78, Jaccard 0.78, H-bond role recall 0.40
Burial
68%
Hydrophobic fit
83%
Reason: no major geometry red flags detected
3 protein-contact clashes 3 intramolecular clashes 48% of hydrophobic surface appears solvent-exposed (11/23 atoms). Partial exposure is common but may limit selectivity and membrane permeability.
Molecular report
Full metrics ↗
Weak Marginal quality. Consider only alongside better-scoring alternatives.
✓ Excellent LE (-0.664 kcal/mol/HA) ✓ Good fit quality (FQ -6.53) ✓ Deep burial (68% SASA buried) ✓ Lipophilic contacts well-matched (83%) ✗ High strain energy (29.2 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (12)
Score
-21.257
kcal/mol
LE
-0.664
kcal/mol/HA
Fit Quality
-6.53
FQ (Leeson)
HAC
32
heavy atoms
MW
470
Da
LogP
4.51
cLogP
Final rank
2.2098
rank score
Inter norm
-0.751
normalised
Contacts
14
H-bonds 5
Strain ΔE
29.2 kcal/mol
SASA buried
68%
Lipo contact
83% BSA apolar/total
SASA unbound
746 Ų
Apolar buried
422 Ų

Interaction summary

HBA 2 HY 8 PI 2 CLASH 3

HBD/HBA · H-bonds (geometric)
HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: strict. Residues: 1.

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.
Name5OL0Contacts18
PoseOpen native poseHB0
IFP residues
ASN193 GLN220 GLU192 GLY191 HIS144 HIS222 ILE126 LEU194 LEU226 PHE189 PHE190 PHE199 PHE74 PRO223 THR71 VAL187 VAL188 VAL221
Current overlap14Native recall0.78
Jaccard0.78RMSD-
HB strict2Strict recall0.40
HB same residue+role2HB role recall0.40
HB same residue2HB residue recall0.50

Protein summary

287 residues
Protein targetT11Atoms4391
Residues287Chains1
Residue summaryLEU:627; ARG:432; VAL:384; GLU:316; PHE:300; ILE:285; ALA:260; PRO:238; HIS:187; ASP:157; LYS:154; SER:154; THR:154; GLY:147; ASN:140; TYR:126

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
124 2.209772416141404 -0.7511 -21.2566 5 14 14 0.78 0.40 - no Current
80 4.583978725486131 -0.806529 -16.5729 8 16 0 0.00 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 -21.257kcal/mol
Ligand efficiency (LE) -0.6643kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -6.532
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 32HA

Physicochemical properties
Molecular weight 469.6Da
Lipinski: ≤ 500 Da
LogP (cLogP) 4.51
Lipinski: ≤ 5
Rotatable bonds 7

Conformational strain (MMFF94s)
Strain energy (ΔE) 29.18kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 89.88kcal/mol
Minimised FF energy 60.69kcal/mol

SASA & burial

✓ computed
SASA (unbound) 746.4Ų
Total solvent-accessible surface area of free ligand
BSA total 508.4Ų
Buried surface area upon binding
BSA apolar 422.2Ų
Hydrophobic contacts buried
BSA polar 86.3Ų
Polar contacts buried
Fraction buried 68.1%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 83.0%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2013.0Ų
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 2380.0Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 977.8Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)