Docking pose detail

Molecular metrics status: done

RDKit SASA-based burial metrics are cached.

SASA cached

T11

L. infantum SIR2 L. infantum

Ligand OSA_Lib_88

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 mixed SASA done

Strain ΔE

45.2 kcal/mol

Protein clashes

Internal clashes

Native overlap

contact recall 0.50, Jaccard 0.36, H-bond role recall 0.00

Burial

83%

Hydrophobic fit

94%

Reason: strain 45.2 kcal/mol

strain ΔE 45.2 kcal/mol 1 protein-contact clashes 45% of hydrophobic surface appears solvent-exposed (14/31 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 (-0.576 kcal/mol/HA) ✓ Good fit quality (FQ -5.85) ✓ Deep burial (83% SASA buried) ✓ Lipophilic contacts well-matched (94%) ✗ Extreme strain energy (45.2 kcal/mol) ✗ Geometry warnings ✗ Minor protein-contact clashes (2) ✗ Many internal clashes (17)

Score

-20.734

kcal/mol

-0.576

kcal/mol/HA

Fit Quality

-5.85

FQ (Leeson)

HAC

heavy atoms

488

LogP

2.52

cLogP

Final rank

1.6302

rank score

Inter norm

-0.682

normalised

Contacts

H-bonds 1

Strain ΔE

45.2 kcal/mol

SASA buried

83%

Lipo contact

94% BSA apolar/total

SASA unbound

807 Å²

Apolar buried

632 Å²

Interaction summary

HBA 1 HY 8 PI 2 CLASH 1

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.

Name	5OL0	Contacts	18
Pose	Open native pose	HB	0
IFP residues	ASN193 GLN220 GLU192 GLY191 HIS144 HIS222 ILE126 LEU194 LEU226 PHE189 PHE190 PHE199 PHE74 PRO223 THR71 VAL187 VAL188 VAL221
Current overlap	9	Native recall	0.50
Jaccard	0.36	RMSD	-
HB strict	0	Strict recall	0.00
HB same residue+role	0	HB role recall	0.00
HB same residue	0	HB residue recall	0.00

Protein summary

287 residues

Protein target	T11	Atoms	4391
Residues	287	Chains	1
Residue summary	LEU: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

Pose	Final rank	Inter norm	Score	HB	CT	CT overlap	CT recall	HB role rec.	RMSD	Excluded
159	1.6301743624500802	-0.682445	-20.7341	1	16	9	0.50	0.00	-	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 -20.734kcal/mol

Ligand efficiency (LE) -0.5759kcal/mol/HA

Score / heavy atom count

Fit quality (FQ) -5.854

LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe

Heavy atom count 36HA

Physicochemical properties

Molecular weight 487.7Da

Lipinski: ≤ 500 Da

LogP (cLogP) 2.52

Lipinski: ≤ 5

Rotatable bonds 6

Conformational strain (MMFF94s)

Strain energy (ΔE) 45.22kcal/mol

< 5 good · 5–10 marginal · > 10 problematic

Docked FF energy 172.47kcal/mol

Minimised FF energy 127.25kcal/mol

SASA & burial

✓ computed

SASA (unbound) 807.2Å²

Total solvent-accessible surface area of free ligand

BSA total 669.7Å²

Buried surface area upon binding

BSA apolar 631.7Å²

Hydrophobic contacts buried

BSA polar 38.0Å²

Polar contacts buried

Fraction buried 83.0%

> 60 % indicates good pocket engagement

Lipophilic contact ratio 94.3%

BSA apolar / BSA total — high = hydrophobic driver

Δ Non-polar SASA -2213.9Å²

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 2380.0Å²

Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)

Complex non-polar SASA 928.9Å²

Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)