FAIRMol

NMT-TY0602

Pose ID 14523 Compound 643 Pose 285

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 NMT-TY0602

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Weak SASA cached
Promising but geometrically suspicious
Binding strong Geometry low Native strong SASA done
Strain ΔE
35.3 kcal/mol
Protein clashes
11
Internal clashes
11
Native overlap
contact recall 0.57, Jaccard 0.40, H-bond role recall 0.36
Burial
94%
Hydrophobic fit
57%
Reason: 11 protein-contact clashes, 11 internal clashes
11 protein-contact clashes 11 intramolecular clashes 83% of hydrophobic surface is solvent-exposed (10/12 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 (-1.325 kcal/mol/HA) ✓ Good fit quality (FQ -11.88) ✓ Strong H-bond network (16 bonds) ✓ Deep burial (94% SASA buried) ✗ Very high strain energy (35.3 kcal/mol) ✗ Geometry warnings ✗ Internal clashes (8)
Score
-31.810
kcal/mol
LE
-1.325
kcal/mol/HA
Fit Quality
-11.88
FQ (Leeson)
HAC
24
heavy atoms
MW
371
Da
LogP
0.32
cLogP
Strain ΔE
35.3 kcal/mol
SASA buried
94%
Lipo contact
57% BSA apolar/total
SASA unbound
562 Ų
Apolar buried
302 Ų

Interaction summary

HB 16 HY 3 PI 0 CLASH 11 ⚠ Exposure 83%

HB · H-bonds

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

PI · π–π interactions

No pi · π–π interactions detected for this pose.

HY · Hydrophobic contacts

CLASH · Clashes

🚨Solvent-exposed hydrophobic surface — desolvation penalty likely
83% of hydrophobic surface is solvent-exposed (10/12 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 12 Buried (contacted) 2 Exposed 10 LogP 0.32 H-bonds 16
Exposed fragments: phenyl (6/6 atoms exposed)phenyl (4/6 atoms exposed)
Final rank5.826Score-31.810
Inter norm-1.335Intra norm0.009
Top1000noExcludedno
Contacts21H-bonds16
Artifact reasongeometry warning; 8 clashes; 3 protein clashes; high strain Δ 35.3
Residues
ALA24 ALA70 ASP68 GLN42 GLU21 GLU73 GLY23 GLY25 GLY47 GLY71 ILE46 LEU31 LEU39 LYS26 PHE38 SER22 SER27 SER28 THR44 THR45 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 overlap12Native recall0.57
Jaccard0.40RMSD-
HB strict6Strict recall0.40
HB same residue+role4HB role recall0.36
HB same residue4HB residue recall0.36

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
345 2.3852300086674956 -1.22883 -27.1471 9 14 0 0.00 0.00 - no Open
314 2.517801636797984 -0.942176 -24.1381 5 13 0 0.00 0.00 - no Open
272 2.9189537056135753 -1.1672 -29.7247 13 13 0 0.00 0.00 - no Open
414 3.1764200655621546 -1.06469 -24.8485 7 16 0 0.00 0.00 - no Open
297 3.248504433051989 -0.969391 -16.4093 6 17 0 0.00 0.00 - no Open
274 3.710791772393639 -1.07629 -24.7513 9 15 0 0.00 0.00 - no Open
383 3.8800478154472353 -1.20228 -28.5869 11 16 0 0.00 0.00 - no Open
258 4.050558324957515 -1.18293 -28.8656 12 22 0 0.00 0.00 - no Open
259 4.168971048980509 -1.13785 -26.3976 11 13 0 0.00 0.00 - no Open
364 4.531136784780454 -1.24281 -28.4071 7 15 0 0.00 0.00 - no Open
247 4.9387540833797265 -1.05098 -20.2639 12 13 0 0.00 0.00 - no Open
285 5.825536396152312 -1.3346 -31.8099 16 21 12 0.57 0.36 - 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 -31.810kcal/mol
Ligand efficiency (LE) -1.3254kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -11.878
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 24HA

Physicochemical properties

Molecular weight 371.4Da
Lipinski: ≤ 500 Da
LogP (cLogP) 0.32
Lipinski: ≤ 5
Rotatable bonds 8

Conformational strain (MMFF94s)

Strain energy (ΔE) 35.34kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy -43.33kcal/mol
Minimised FF energy -78.68kcal/mol

SASA & burial

✓ computed
SASA (unbound) 562.4Ų
Total solvent-accessible surface area of free ligand
BSA total 528.5Ų
Buried surface area upon binding
BSA apolar 302.4Ų
Hydrophobic contacts buried
BSA polar 226.2Ų
Polar contacts buried
Fraction buried 94.0%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 57.2%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -1197.0Ų
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 1368.5Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 500.3Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)