FAIRMol

OSA_Lib_189

Pose ID 14388 Compound 5548 Pose 150

DB SELECTIONDocking pose analysis is being read from this database.
Molecular metrics status: done
RDKit SASA-based burial metrics are cached.
SASA cached
T22
L. donovani rab5a L. donovani
Ligand OSA_Lib_189

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
26.7 kcal/mol
Protein clashes
5
Internal clashes
5
Native overlap
contact recall 0.81, Jaccard 0.61, H-bond role recall 0.18
Burial
86%
Hydrophobic fit
96%
Reason: no major geometry red flags detected
5 protein-contact clashes 5 intramolecular clashes 65% of hydrophobic surface is solvent-exposed (20/31 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 ↗
Weak Marginal quality. Consider only alongside better-scoring alternatives.
✓ Excellent LE (-0.881 kcal/mol/HA) ✓ Good fit quality (FQ -8.95) ✓ Good H-bonds (4 bonds) ✓ Deep burial (86% SASA buried) ✓ Lipophilic contacts well-matched (96%) ✗ High strain energy (26.7 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (17)
Score
-31.706
kcal/mol
LE
-0.881
kcal/mol/HA
Fit Quality
-8.95
FQ (Leeson)
HAC
36
heavy atoms
MW
489
Da
LogP
1.10
cLogP
Strain ΔE
26.7 kcal/mol
SASA buried
86%
Lipo contact
96% BSA apolar/total
SASA unbound
794 Ų
Apolar buried
659 Ų

Interaction summary

HB 4 HY 7 PI 1 CLASH 5 ⚠ Exposure 64%

HB · H-bonds

Mode: strict. Count shows atom-level H-bonds; unique residues in summary: 0.

PI · π–π interactions

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

HY · Hydrophobic contacts

CLASH · Clashes

🚨Solvent-exposed hydrophobic surface — desolvation penalty likely
65% of hydrophobic surface is solvent-exposed (20/31 atoms). Large non-polar area without protein contacts incurs a desolvation penalty and will reduce binding affinity. Consider truncating or replacing the exposed fragment.
Non-polar atoms 31 Buried (contacted) 11 Exposed 20 LogP 1.1 H-bonds 4
Exposed fragments: phenyl (6/6 atoms exposed)phenyl (6/6 atoms exposed)phenyl (6/6 atoms exposed)phenyl (4/5 atoms exposed)phenyl (6/6 atoms exposed)aliphatic chain/group (2 atoms exposed)
Final rank4.406Score-31.706
Inter norm-0.867Intra norm-0.014
Top1000noExcludedno
Contacts24H-bonds4
Artifact reasongeometry warning; 17 clashes; 2 protein clashes; moderate strain Δ 26.7
Residues
ALA158 ALA24 ALA40 ALA70 ASN126 ASN41 ASP68 GLN42 GLU73 GLY23 GLY25 GLY47 GLY71 LEU31 LEU39 LYS127 LYS159 LYS26 PHE38 SER22 SER27 SER28 THR44 THR69

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
Jaccard0.61RMSD-
HB strict3Strict recall0.20
HB same residue+role2HB role recall0.18
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
150 4.405682428734045 -0.866518 -31.7059 4 24 17 0.81 0.18 - 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 -31.706kcal/mol
Ligand efficiency (LE) -0.8807kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -8.951
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 36HA

Physicochemical properties

Molecular weight 488.7Da
Lipinski: ≤ 500 Da
LogP (cLogP) 1.10
Lipinski: ≤ 5
Rotatable bonds 6

Conformational strain (MMFF94s)

Strain energy (ΔE) 26.68kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 225.33kcal/mol
Minimised FF energy 198.65kcal/mol

SASA & burial

✓ computed
SASA (unbound) 794.4Ų
Total solvent-accessible surface area of free ligand
BSA total 684.4Ų
Buried surface area upon binding
BSA apolar 659.2Ų
Hydrophobic contacts buried
BSA polar 25.1Ų
Polar contacts buried
Fraction buried 86.1%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 96.3%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -1617.9Ų
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 519.8Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)