FAIRMol

NMT-TY0705

Pose ID 8410 Compound 4032 Pose 280

DB fairmolDocking pose analysis is being read from this database.
Molecular metrics status: done
RDKit SASA-based burial metrics are cached.
SASA cached
T13
T. brucei ODC (Active site) T. brucei Active site
Ligand NMT-TY0705
PDB1F3T

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Promising SASA cached
Promising and worth follow-up
Binding strong Geometry high Native strong SASA done
Strain ΔE
10.0 kcal/mol
Protein clashes
1
Internal clashes
1
Native overlap
contact recall 0.74, Jaccard 0.67, H-bond role recall 0.29
Burial
78%
Hydrophobic fit
77%
Reason: no major geometry red flags detected
1 protein-contact clashes
Molecular report
Full metrics ↗
Promising Reasonable quality metrics. Warrants further investigation.
✓ Excellent LE (-1.269 kcal/mol/HA) ✓ Good fit quality (FQ -10.82) ✓ Strong H-bond network (7 bonds) ✓ Deep burial (78% SASA buried) ✓ Lipophilic contacts well-matched (77%) ✗ Moderate strain (10.0 kcal/mol) ✗ Geometry warnings ✗ Internal clashes (7)
Score
-26.641
kcal/mol
LE
-1.269
kcal/mol/HA
Fit Quality
-10.82
FQ (Leeson)
HAC
21
heavy atoms
MW
304
Da
LogP
2.00
cLogP
Final rank
3.7753
rank score
Inter norm
-1.338
normalised
Contacts
16
H-bonds 8
Strain ΔE
10.0 kcal/mol
SASA buried
78%
Lipo contact
77% BSA apolar/total
SASA unbound
546 Ų
Apolar buried
327 Ų

Interaction summary

HBD 2 HBA 5 HY 3 PI 2 CLASH 1

HBD/HBA · H-bonds (geometric)

HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: permissive. Residues: 5.

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: permissive.
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 overlap14Native recall0.74
Jaccard0.67RMSD-
HB strict3Strict recall0.33
HB same residue+role2HB role recall0.29
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
335 1.5194967487690838 -1.0163 -20.0666 4 13 0 0.00 0.00 - no Open
300 1.6846590432116946 -1.01232 -20.1901 4 13 0 0.00 0.00 - no Open
280 3.7752707121830755 -1.33779 -26.6408 8 16 14 0.74 0.29 - no Current
237 3.875077357919454 -1.33963 -26.5646 8 16 14 0.74 0.29 - 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 -26.641kcal/mol
Ligand efficiency (LE) -1.2686kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -10.821
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 21HA

Physicochemical properties

Molecular weight 304.4Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.00
Lipinski: ≤ 5
Rotatable bonds 4

Conformational strain (MMFF94s)

Strain energy (ΔE) 9.97kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy -66.84kcal/mol
Minimised FF energy -76.81kcal/mol

SASA & burial

✓ computed
SASA (unbound) 546.0Ų
Total solvent-accessible surface area of free ligand
BSA total 424.6Ų
Buried surface area upon binding
BSA apolar 326.7Ų
Hydrophobic contacts buried
BSA polar 97.9Ų
Polar contacts buried
Fraction buried 77.8%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 76.9%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2492.6Ų
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 1392.4Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)