FAIRMol

KB_HAT_184

Pose ID 8209 Compound 1859 Pose 79

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
T13
T. brucei ODC (Active site) T. brucei Active site
Ligand KB_HAT_184
PDB1F3T↗

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
34.2 kcal/mol
Protein clashes
2
Internal clashes
2
Native overlap
contact recall 0.58, Jaccard 0.44, H-bond role recall 0.43
Burial
84%
Hydrophobic fit
70%
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 (-0.910 kcal/mol/HA) ✓ Good fit quality (FQ -8.38) ✓ Strong H-bond network (7 bonds) ✓ Deep burial (84% SASA buried) ✓ Lipophilic contacts well-matched (70%) ✗ Very high strain energy (34.2 kcal/mol) ✗ Geometry warnings ✗ Internal clashes (9)
Score
-23.662
kcal/mol
LE
-0.910
kcal/mol/HA
Fit Quality
-8.38
FQ (Leeson)
HAC
26
heavy atoms
MW
344
Da
LogP
2.60
cLogP
Final rank
2.2238
rank score
Inter norm
-1.192
normalised
Contacts
17
H-bonds 9
Strain ΔE
34.2 kcal/mol
SASA buried
84%
Lipo contact
70% BSA apolar/total
SASA unbound
569 Ų
Apolar buried
337 Ų

Interaction summary

HBA 7 HY 3 PI 3 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.
Name1F3TContacts19
PoseOpen native poseHB0
IFP residues
ALA111 ALA67 ARG154 ARG277 ASP332 ASP88 CYS70 GLU274 GLY236 GLY237 GLY276 HIS197 LYS69 PHE238 PRO275 SER200 TYR278 TYR331 TYR389
Current overlap11Native recall0.58
Jaccard0.44RMSD-
HB strict4Strict recall0.44
HB same residue+role3HB role recall0.43
HB same residue3HB residue recall0.43

Protein summary

411 residues
Protein targetT13Atoms6340
Residues411Chains1
Residue summaryVAL:624; LEU:551; LYS:506; ARG:480; PHE:460; ILE:418; ASP:348; GLU:332; THR:322; TYR:315; PRO:308; ALA:290; SER:264; GLY:224; ASN:210; GLN:170

All stored poses for this docking hit

PoseFinal rankInter normScoreHBCTCT overlapCT recallHB role rec.RMSDExcluded
62 1.832372404293249 -1.0853 -22.0823 4 13 0 0.00 0.00 - no Open
114 2.057436947918806 -0.795235 -15.1942 4 12 0 0.00 0.00 - no Open
79 2.2238271761561177 -1.19184 -23.6622 9 17 11 0.58 0.43 - no Current
86 3.690209156460258 -1.06174 -24.433 10 18 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 -23.662kcal/mol
Ligand efficiency (LE) -0.9101kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -8.385
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 26HA

Physicochemical properties
Molecular weight 344.3Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.60
Lipinski: ≤ 5
Rotatable bonds 3

Conformational strain (MMFF94s)
Strain energy (ΔE) 34.24kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy -43.29kcal/mol
Minimised FF energy -77.53kcal/mol

SASA & burial

✓ computed
SASA (unbound) 569.2Ų
Total solvent-accessible surface area of free ligand
BSA total 480.4Ų
Buried surface area upon binding
BSA apolar 337.0Ų
Hydrophobic contacts buried
BSA polar 143.3Ų
Polar contacts buried
Fraction buried 84.4%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 70.2%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2486.1Ų
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 3461.2Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 1390.3Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)