FAIRMol

TC484

Pose ID 13795 Compound 5402 Pose 237

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
T21
T. cruzi R5P T. cruzi
Ligand TC484
PDB3K7O↗

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
40.6 kcal/mol
Protein clashes
1
Internal clashes
1
Native overlap
contact recall 0.86, Jaccard 0.57, H-bond role recall 0.22
Burial
65%
Hydrophobic fit
88%
Reason: no major geometry red flags detected
1 protein-contact clashes 62% of hydrophobic surface is solvent-exposed (20/32 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.
✓ Good LE (-0.383 kcal/mol/HA) ✓ Good fit quality (FQ -4.03) ✓ Good H-bonds (5 bonds) ✓ Good burial (65% SASA buried) ✓ Lipophilic contacts well-matched (88%) ✗ Extreme strain energy (40.6 kcal/mol) ✗ Geometry warnings ✗ Protein-contact clashes (6) ✗ Many internal clashes (17)
Score
-15.706
kcal/mol
LE
-0.383
kcal/mol/HA
Fit Quality
-4.03
FQ (Leeson)
HAC
41
heavy atoms
MW
559
Da
LogP
5.24
cLogP
Final rank
2.2798
rank score
Inter norm
-0.600
normalised
Contacts
19
H-bonds 7
Strain ΔE
40.6 kcal/mol
SASA buried
65%
Lipo contact
88% BSA apolar/total
SASA unbound
924 Ų
Apolar buried
524 Ų

Interaction summary

HBA 5 HY 2 PI 2 CLASH 1

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.
Name3K7OContacts14
PoseOpen native poseHB0
IFP residues
ARG137 ARG141 ASN103 HIS102 HIS138 ASP10 CYS69 GLY70 GLY74 HIS11 ILE73 PRO12 SER71 TYR46
Current overlap12Native recall0.86
Jaccard0.57RMSD-
HB strict2Strict recall0.17
HB same residue+role2HB role recall0.22
HB same residue2HB residue recall0.25

Protein summary

305 residues
Protein targetT21Atoms4646
Residues305Chains2
Residue summaryARG:576; ILE:532; VAL:512; GLU:420; ALA:360; PHE:240; HIS:238; LYS:220; THR:210; LEU:190; PRO:168; TYR:168; GLY:154; SER:154; ASP:144; ASN:112

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
237 2.2797576269640536 -0.600431 -15.7056 7 19 12 0.86 0.22 - 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 -15.706kcal/mol
Ligand efficiency (LE) -0.3831kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -4.025
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 41HA

Physicochemical properties
Molecular weight 558.7Da
Lipinski: ≤ 500 Da
LogP (cLogP) 5.24
Lipinski: ≤ 5
Rotatable bonds 12

Conformational strain (MMFF94s)
Strain energy (ΔE) 40.64kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 142.47kcal/mol
Minimised FF energy 101.83kcal/mol

SASA & burial

✓ computed
SASA (unbound) 924.0Ų
Total solvent-accessible surface area of free ligand
BSA total 598.3Ų
Buried surface area upon binding
BSA apolar 523.6Ų
Hydrophobic contacts buried
BSA polar 74.7Ų
Polar contacts buried
Fraction buried 64.8%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 87.5%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2508.7Ų
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 2482.0Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 775.6Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)