FAIRMol

TC232

Pose ID 14434 Compound 5285 Pose 196

DB SELECTIONDocking 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 TC232

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Reject SASA cached
Likely artefact or unreliable pose
Binding strong Geometry medium Native strong SASA done
Strain ΔE
36.0 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.62, Jaccard 0.43, H-bond role recall 0.18
Burial
89%
Hydrophobic fit
82%
Reason: no major geometry red flags detected
2 protein-contact clashes 75% of hydrophobic surface is solvent-exposed (15/20 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 ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-1.024 kcal/mol/HA) ✓ Good fit quality (FQ -9.66) ✓ Strong H-bond network (6 bonds) ✓ Deep burial (89% SASA buried) ✓ Lipophilic contacts well-matched (82%) ✗ Very high strain energy (36.0 kcal/mol) ✗ Geometry warnings ✗ Protein-contact clashes (7) ✗ Many internal clashes (15)
Score
-28.658
kcal/mol
LE
-1.024
kcal/mol/HA
Fit Quality
-9.66
FQ (Leeson)
HAC
28
heavy atoms
MW
402
Da
LogP
0.07
cLogP
Final rank
1.6900
rank score
Inter norm
-1.097
normalised
Contacts
22
H-bonds 8
Strain ΔE
36.0 kcal/mol
SASA buried
89%
Lipo contact
82% BSA apolar/total
SASA unbound
658 Ų
Apolar buried
481 Ų

Interaction summary

HBD 4 HBA 2 HY 3 PI 0 CLASH 2

HBD/HBA · H-bonds (geometric)
HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: strict. Residues: 4.

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

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 overlap13Native recall0.62
Jaccard0.43RMSD-
HB strict2Strict recall0.13
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
196 1.6900078924575355 -1.09693 -28.6576 8 22 13 0.62 0.18 - no Current
265 3.9303977783143753 -0.687515 -19.2256 5 13 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 -28.658kcal/mol
Ligand efficiency (LE) -1.0235kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -9.662
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 28HA

Physicochemical properties
Molecular weight 401.5Da
Lipinski: ≤ 500 Da
LogP (cLogP) 0.07
Lipinski: ≤ 5
Rotatable bonds 7

Conformational strain (MMFF94s)
Strain energy (ΔE) 36.03kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 48.04kcal/mol
Minimised FF energy 12.01kcal/mol

SASA & burial

✓ computed
SASA (unbound) 657.5Ų
Total solvent-accessible surface area of free ligand
BSA total 584.0Ų
Buried surface area upon binding
BSA apolar 481.3Ų
Hydrophobic contacts buried
BSA polar 102.7Ų
Polar contacts buried
Fraction buried 88.8%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 82.4%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -1421.1Ų
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 501.4Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)