FAIRMol

OHD_Leishmania_125

Pose ID 12920 Compound 344 Pose 67

DB Docking_panel_21Docking pose analysis is being read from this database.
Molecular metrics status: done
Cached molecular metrics are available for this pose.
Metrics cached · SASA missing

py3Dmol interaction viewer

Left: interactive complex viewer. Right: clickable PLIP-like interaction summary. Clicking an interaction thickens and highlights it in the 3D view.
Strict H-bonds Permissive H-bonds
Molecular report
Full metrics ↗
Reject Multiple quality flags — this pose should be deprioritised or discarded.
✓ Excellent LE (-1.089 kcal/mol/HA) ✓ Good fit quality (FQ -11.30) ✓ Strong H-bond network (8 bonds) ✗ Very high strain energy (41.5 kcal/mol) ✗ Geometry warnings ✗ Protein contact clashes ℹ SASA not computed
Score
-42.481
kcal/mol
LE
-1.089
kcal/mol/HA
Fit Quality
-11.30
FQ (Leeson)
HAC
39
heavy atoms
MW
528
Da
LogP
2.24
cLogP
Strain ΔE
41.5 kcal/mol
SASA buried
computing…
Overall: Promising but geometrically suspicious
Binding evidence: strong
Native-like contacts: strong
Ligand efficiency: excellent
Geometry reliability: low
Reason: geometry warning, clashes, protein contact clashes, strain 41.5 kcal/mol

Interaction summary

Collapsible panels
H-bonds 8 Hydrophobic 24 π–π 4 Clashes 6 Severe clashes 0
Final rank7.105491336351991Score-42.481
Inter norm-1.01165Intra norm-0.0776061
Top1000noExcludedno
Contacts21H-bonds8
Artifact reasongeometry warning; 21 clashes; 6 protein contact clashes; high strain Δ 44.6
ResiduesA:ALA96;A:ARG14;A:ASP161;A:CYS168;A:GLY205;A:LEU208;A:LEU209;A:LEU263;A:MET163;A:MET213;A:NAP301;A:PHE171;A:PHE97;A:PRO210;A:PRO99;A:SER207;A:SER95;A:TRP221;A:TYR174;A:TYR98;A:VAL206

Protein summary

258 residues
Protein targetT08Atoms3881
Residues258Chains2
Residue summaryLEU:437; VAL:433; ALA:361; ARG:288; ILE:266; GLU:210; LYS:198; SER:198; ASN:182; THR:154; GLN:153; PHE:140; PRO:140; TYR:126; GLY:112; HIS:103

Native ligand reference

★ reference
Interaction fingerprint calculated directly from the uploaded native ligand without docking. Current H-bond mode: strict.
NameTbPTR1_cW_6RX6_ReadyContacts19
PoseOpen native poseH-bonds6
IFP residuesA:ARG14; A:ASP161; A:CYS168; A:GLY205; A:LEU208; A:LEU209; A:LYS178; A:MET213; A:NAP301; A:PHE171; A:PHE97; A:PRO210; A:PRO99; A:SER207; A:SER95; A:TRP221; A:TYR174; A:TYR98; A:VAL206
Current overlap18Native recall0.95
Jaccard0.82RMSD-
H-bond strict5Strict recall0.83
H-bond same residue+role4Role recall0.80
H-bond same residue4Residue recall0.80

Hydrogen bonds

Mode: strict. Count shows atom-level H-bonds; unique residues in summary: 0.

π–π interactions

Native π–π recall is disabled because no explicit native π–π reference was stored.

Hydrophobic contacts

Clashes

All stored poses for this docking hit

PoseFinal rankInter normScoreHBContactsNative overlapNative recallHB role recallRMSDExcluded
53 5.952902632390996 -0.688344 -23.1565 3 22 0 0.00 0.00 - no Open
66 6.335672379969568 -0.958393 -39.6868 7 20 18 0.95 0.80 - no Open
67 7.105491336351991 -1.01165 -42.481 8 21 18 0.95 0.80 - no Current
68 7.8518924943628345 -1.05532 -40.4499 7 19 17 0.89 0.80 - no Open
54 8.932909712604019 -0.667498 -23.843 8 20 0 0.00 0.00 - yes Open
55 9.542279069114752 -0.651804 -17.3114 6 23 0 0.00 0.00 - yes Open

Molecular metrics

FreeSASA-based burial, strain energy (MMFF94s), ligand efficiency and fit quality for this docking pose.
✓ Metrics available

Scoring & efficiency

Docking score -42.481kcal/mol
Ligand efficiency (LE) -1.0893kcal/mol/HA
Score / heavy atom count
Fit quality (FQ) -11.304
LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe
Heavy atom count 39HA

Physicochemical properties

Molecular weight 527.6Da
Lipinski: ≤ 500 Da
LogP (cLogP) 2.24
Lipinski: ≤ 5
Rotatable bonds 7

Conformational strain (MMFF94s)

Strain energy (ΔE) 41.47kcal/mol
< 5 good · 5–10 marginal · > 10 problematic
Docked FF energy 109.27kcal/mol
Minimised FF energy 67.80kcal/mol

SASA & burial (FreeSASA)

not yet run
SASA has not been computed yet for this pose. Queue a background recompute to populate FreeSASA burial metrics without blocking the page.