FAIRMol

OSA_Lib_303

Pose ID 14397 Compound 3614 Pose 159

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
T22
L. donovani rab5a L. donovani
Ligand OSA_Lib_303

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 high Native strong SASA done
Strain ΔE
15.8 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.81, Jaccard 0.71, H-bond role recall 0.09
Burial
92%
Hydrophobic fit
95%
Reason: no major geometry red flags detected
2 protein-contact clashes 56% of hydrophobic surface appears solvent-exposed (15/27 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 (-0.993 kcal/mol/HA) ✓ Good fit quality (FQ -9.58) ✓ Good H-bonds (3 bonds) ✓ Deep burial (92% SASA buried) ✓ Lipophilic contacts well-matched (95%) ✗ Moderate strain (15.8 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (13)
Score
-29.783
kcal/mol
LE
-0.993
kcal/mol/HA
Fit Quality
-9.58
FQ (Leeson)
HAC
30
heavy atoms
MW
399
Da
LogP
3.42
cLogP
Final rank
2.2161
rank score
Inter norm
-1.012
normalised
Contacts
20
H-bonds 4
Strain ΔE
15.8 kcal/mol
SASA buried
92%
Lipo contact
95% BSA apolar/total
SASA unbound
677 Ų
Apolar buried
592 Ų

Interaction summary

HBD 1 HBA 2 HY 4 PI 1 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
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.
NameRAB5AContacts21
PoseOpen native poseHB0
IFP residues
ALA158 ALA24 ALA40 ASN126 ASN41 ASP129 GLN42 GLU21 GLU73 GLY23 GLY25 LEU130 LEU39 LYS127 LYS159 LYS26 PHE38 SER157 SER22 SER27 SER28
Current overlap17Native recall0.81
Jaccard0.71RMSD-
HB strict1Strict recall0.07
HB same residue+role1HB role recall0.09
HB same residue2HB residue recall0.18

Protein summary

165 residues
Protein targetT22Atoms2561
Residues165Chains1
Residue summaryLEU:363; LYS:242; ALA:231; ARG:214; ILE:190; GLU:180; VAL:144; SER:143; PHE:140; ASN:112; THR:112; TYR:105; GLN:102; ASP:96; GLY:77; TRP:48

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
167 0.7603671833333169 -0.8127 -22.1851 1 17 1 0.05 0.00 - no Open
159 2.2161257495746955 -1.01216 -29.7833 4 20 17 0.81 0.09 - 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 -29.783kcal/mol
Ligand efficiency (LE) -0.9928kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -9.577
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 30HA

Physicochemical properties
Molecular weight 398.6Da
Lipinski: ≤ 500 Da
LogP (cLogP) 3.42
Lipinski: ≤ 5
Rotatable bonds 5

Conformational strain (MMFF94s)
Strain energy (ΔE) 15.78kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 86.85kcal/mol
Minimised FF energy 71.06kcal/mol

SASA & burial

✓ computed
SASA (unbound) 677.2Ų
Total solvent-accessible surface area of free ligand
BSA total 622.6Ų
Buried surface area upon binding
BSA apolar 592.1Ų
Hydrophobic contacts buried
BSA polar 30.5Ų
Polar contacts buried
Fraction buried 91.9%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 95.1%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -1526.4Ų
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 1368.5Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 488.8Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)