FAIRMol

OHD_MAC_3

Pose ID 8445 Compound 3343 Pose 315

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 OHD_MAC_3
PDB1F3T↗

3D complex viewer

Strict H-bonds Permissive H-bonds
Viewer legend
Protein receptor
Pocket residues
Cofactor context
Docked ligand
Overall assessment
Reject SASA cached
Promising but geometrically suspicious
Binding strong Geometry low Native strong SASA done
Strain ΔE
61.5 kcal/mol
Protein clashes
8
Internal clashes
8
Native overlap
contact recall 0.84, Jaccard 0.62, H-bond role recall 0.71
Burial
79%
Hydrophobic fit
79%
Reason: 8 internal clashes, strain 61.5 kcal/mol
strain ΔE 61.5 kcal/mol 8 protein-contact clashes 8 intramolecular clashes
Molecular report
Full metrics ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-0.532 kcal/mol/HA) ✓ Good fit quality (FQ -5.45) ✓ Strong H-bond network (11 bonds) ✓ Deep burial (79% SASA buried) ✓ Lipophilic contacts well-matched (79%) ✗ Extreme strain energy (61.5 kcal/mol) ✗ Geometry warnings ✗ Many internal clashes (19)
Score
-19.687
kcal/mol
LE
-0.532
kcal/mol/HA
Fit Quality
-5.45
FQ (Leeson)
HAC
37
heavy atoms
MW
498
Da
LogP
1.78
cLogP
Final rank
5.3944
rank score
Inter norm
-0.853
normalised
Contacts
23
H-bonds 16
Strain ΔE
61.5 kcal/mol
SASA buried
79%
Lipo contact
79% BSA apolar/total
SASA unbound
816 Ų
Apolar buried
510 Ų

Interaction summary

HBD 3 HBA 8 HY 3 PI 4 CLASH 8

HBD/HBA · H-bonds (geometric)
HBD = ligand donates H · HBA = ligand accepts H · ~ = weak (≥110°). Mode: strict. Residues: 8.

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 overlap16Native recall0.84
Jaccard0.62RMSD-
HB strict6Strict recall0.67
HB same residue+role5HB role recall0.71
HB same residue5HB residue recall0.71

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
353 3.6605677573847943 -0.763663 -12.0365 6 17 0 0.00 0.00 - no Open
353 4.39998033803745 -0.769384 -12.8873 11 17 0 0.00 0.00 - no Open
313 4.758383907657859 -0.85718 -25.4287 15 20 0 0.00 0.00 - no Open
315 5.394403083352138 -0.852659 -19.6874 16 23 16 0.84 0.71 - no Current
344 5.514129269968441 -0.838101 -15.2066 11 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 -19.687kcal/mol
Ligand efficiency (LE) -0.5321kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -5.448
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 37HA

Physicochemical properties
Molecular weight 497.5Da
Lipinski: ≤ 500 Da
LogP (cLogP) 1.78
Lipinski: ≤ 5
Rotatable bonds 11

Conformational strain (MMFF94s)
Strain energy (ΔE) 61.55kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 129.80kcal/mol
Minimised FF energy 68.25kcal/mol

SASA & burial

✓ computed
SASA (unbound) 815.8Ų
Total solvent-accessible surface area of free ligand
BSA total 647.8Ų
Buried surface area upon binding
BSA apolar 509.6Ų
Hydrophobic contacts buried
BSA polar 138.2Ų
Polar contacts buried
Fraction buried 79.4%
> 60 % indicates good pocket engagement
Lipophilic contact ratio 78.7%
BSA apolar / BSA total — high = hydrophobic driver
Δ Non-polar SASA -2699.4Ų
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 3461.2Ų
Non-polar SASA of receptor alone (VdW proxy, nonpolar atoms only)
Complex non-polar SASA 1404.8Ų
Non-polar SASA of full complex (VdW proxy, nonpolar atoms only)