FAIRMol

Z754931262

Pose ID 10070 Compound 2847 Pose 584

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
T15
T. brucei TR (Dimer cleft site) T. brucei Dimer cleft site
Ligand Z754931262
PDB9IFF↗

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 high Native strong SASA done
Strain ΔE
19.2 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.77, Jaccard 0.53
Burial
66%
Hydrophobic fit
75%
Reason: no major geometry red flags detected
2 protein-contact clashes
Molecular report
Full metrics ↗
Weak Marginal quality. Consider only alongside better-scoring alternatives.
✓ Excellent LE (-0.667 kcal/mol/HA) ✓ Good fit quality (FQ -6.67) ✓ Good H-bonds (3 bonds) ✓ Deep burial (66% SASA buried) ✓ Lipophilic contacts well-matched (75%) ✗ Moderate strain (19.2 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (14)
Score
-22.682
kcal/mol
LE
-0.667
kcal/mol/HA
Fit Quality
-6.67
FQ (Leeson)
HAC
34
heavy atoms
MW
474
Da
LogP
6.08
cLogP
Final rank
3.5841
rank score
Inter norm
-0.741
normalised
Contacts
16
H-bonds 4
Strain ΔE
19.2 kcal/mol
SASA buried
66%
Lipo contact
75% BSA apolar/total
SASA unbound
780 Ų
Apolar buried
387 Ų

Interaction summary

HBD 1 HBA 2 HY 8 PI 1 CLASH 2

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.
Name9IFFContacts13
PoseOpen native poseHB0
IFP residues
ALA209 ARG74 ASN208 GLY214 GLY215 GLY85 LEU73 LYS211 MET70 PHE83 PRO212 PRO213 VAL88
Current overlap10Native recall0.77
Jaccard0.53RMSD-
HB strict0Strict recall-
HB same residue+role0HB role recall-
HB same residue0HB residue recall-

Protein summary

489 residues
Protein targetT15Atoms7420
Residues489Chains1
Residue summaryVAL:768; LYS:704; LEU:703; ILE:532; GLU:450; THR:434; ARG:408; PHE:400; ALA:390; ASN:350; PRO:350; GLY:336; SER:319; TYR:294; ASP:264; MET:204

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
528 1.3019179740781732 -0.828649 -24.1193 9 17 0 0.00 - - no Open
519 1.40595907516357 -0.912231 -27.3828 5 20 0 0.00 - - no Open
563 1.6002195039777414 -0.650692 -10.885 3 12 0 0.00 - - no Open
554 1.6435544364136543 -0.849366 -31.0301 9 15 0 0.00 - - no Open
536 2.4620461084689143 -0.71194 -24.1287 5 13 0 0.00 - - no Open
535 3.099231967304664 -0.933108 -26.6993 6 24 0 0.00 - - no Open
584 3.58412983585218 -0.740743 -22.6816 4 16 10 0.77 - - 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 -22.682kcal/mol
Ligand efficiency (LE) -0.6671kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -6.675
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 34HA

Physicochemical properties
Molecular weight 473.6Da
Lipinski: ≤ 500 Da
LogP (cLogP) 6.08
Lipinski: ≤ 5
Rotatable bonds 9

Conformational strain (MMFF94s)
Strain energy (ΔE) 19.24kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 115.65kcal/mol
Minimised FF energy 96.41kcal/mol

SASA & burial

✓ computed
SASA (unbound) 780.5Ų
Total solvent-accessible surface area of free ligand
BSA total 517.5Ų
Buried surface area upon binding
BSA apolar 387.1Ų
Hydrophobic contacts buried
BSA polar 130.4Ų
Polar contacts buried
Fraction buried 66.3%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 74.8%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -3100.0Ų
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 4005.2Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 1534.1Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)