FAIRMol

MK152

Pose ID 13829 Compound 1283 Pose 271

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 MK152
PDB3K7O↗

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
37.6 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.86, Jaccard 0.75, H-bond role recall 0.67
Burial
55%
Hydrophobic fit
73%
Reason: no major geometry red flags detected
2 protein-contact clashes 68% of hydrophobic surface is solvent-exposed (17/25 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 (-0.564 kcal/mol/HA) ✓ Good fit quality (FQ -5.60) ✓ Strong H-bond network (8 bonds) ✓ Good burial (55% SASA buried) ✓ Lipophilic contacts well-matched (73%) ✗ Very high strain energy (37.6 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (13)
Score
-18.616
kcal/mol
LE
-0.564
kcal/mol/HA
Fit Quality
-5.60
FQ (Leeson)
HAC
33
heavy atoms
MW
454
Da
LogP
3.86
cLogP
Final rank
4.1113
rank score
Inter norm
-0.811
normalised
Contacts
14
H-bonds 13
Strain ΔE
37.6 kcal/mol
SASA buried
55%
Lipo contact
73% BSA apolar/total
SASA unbound
757 Ų
Apolar buried
305 Ų

Interaction summary

HBD 1 HBA 7 HY 1 PI 2 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
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
Jaccard0.75RMSD-
HB strict7Strict recall0.58
HB same residue+role6HB role recall0.67
HB same residue6HB residue recall0.75

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
309 2.3546054172072024 -0.820276 -17.9033 4 18 0 0.00 0.00 - no Open
245 2.4760970820300683 -0.791369 -16.6012 4 20 0 0.00 0.00 - no Open
255 3.5734208585569096 -0.96543 -26.8283 8 17 0 0.00 0.00 - no Open
271 4.111285453773599 -0.811195 -18.6157 13 14 12 0.86 0.67 - 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 -18.616kcal/mol
Ligand efficiency (LE) -0.5641kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -5.597
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 33HA

Physicochemical properties
Molecular weight 453.5Da
Lipinski: ≤ 500 Da
LogP (cLogP) 3.86
Lipinski: ≤ 5
Rotatable bonds 10

Conformational strain (MMFF94s)
Strain energy (ΔE) 37.62kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 79.80kcal/mol
Minimised FF energy 42.18kcal/mol

SASA & burial

✓ computed
SASA (unbound) 756.6Ų
Total solvent-accessible surface area of free ligand
BSA total 415.9Ų
Buried surface area upon binding
BSA apolar 305.2Ų
Hydrophobic contacts buried
BSA polar 110.7Ų
Polar contacts buried
Fraction buried 55.0%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 73.4%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2340.4Ų
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 2482.0Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 766.9Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)