Docking pose detail

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.

✓ Acceptable LE (-0.299 kcal/mol/HA) ✓ Good fit quality (FQ -2.88) ✗ Very high strain energy (23.7 kcal/mol) ✗ No H-bonds detected ✗ Geometry warnings ℹ SASA not computed

Score

-8.965

kcal/mol

-0.299

kcal/mol/HA

Fit Quality

-2.88

FQ (Leeson)

HAC

heavy atoms

405

LogP

4.11

cLogP

Strain ΔE

23.7 kcal/mol

SASA buried

computing…

Overall: Promising but geometrically suspicious

Binding evidence: strong

Native-like contacts: strong

Ligand efficiency: good

Geometry reliability: low

Reason: geometry warning, clashes, strain 23.7 kcal/mol

Interaction summary

Collapsible panels

H-bonds 0 Hydrophobic 24 π–π 1 Clashes 13 Severe clashes 2

Final rank	59.30284108553114	Score	-8.96522
Inter norm	-0.647193	Intra norm	0.348352
Top1000	no	Excluded	yes
Contacts	21	H-bonds	0
Artifact reason	excluded; geometry warning; 17 clashes; 2 protein clashes
Residues	A:ALA10;A:ARG29;A:ASN65;A:ASP22;A:GLU31;A:GLY21;A:ILE61;A:ILE8;A:LEU23;A:LEU28;A:LEU68;A:NAP201;A:PHE32;A:PHE35;A:PRO27;A:PRO62;A:SER60;A:TRP25;A:TYR122;A:VAL116;A:VAL9

Protein summary

200 residues

Protein target	T02	Atoms	3128
Residues	200	Chains	2
Residue summary	LYS:374; LEU:361; GLU:240; VAL:224; ARG:192; PHE:180; ILE:171; PRO:168; ASN:140; SER:132; TYR:126; GLN:119; ASP:108; MET:102; THR:98; GLY:91

Native ligand reference

★ reference

Interaction fingerprint calculated directly from the uploaded native ligand without docking. Current H-bond mode: strict.

Name	5SD8	Contacts	21
Pose	Open native pose	H-bonds	5
IFP residues	A:ALA10; A:ASN65; A:ASP22; A:GLN36; A:GLU31; A:GLY117; A:GLY21; A:ILE61; A:ILE8; A:LEU23; A:LEU68; A:NAP201; A:PHE32; A:PHE35; A:PRO62; A:SER60; A:THR137; A:THR57; A:TYR122; A:VAL116; A:VAL9
Current overlap	17	Native recall	0.81
Jaccard	0.68	RMSD	-
H-bond strict	0	Strict recall	0.00
H-bond same residue+role	0	Role recall	0.00
H-bond same residue	0	Residue recall	0.00

Hydrogen bonds

No hydrogen bonds detected for this pose.

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

Pose	Final rank	Inter norm	Score	HB	Contacts	Native overlap	Native recall	HB role recall	RMSD	Excluded
1222	6.062955738783946	-0.654164	-19.4484	0	20	18	0.86	0.00	-	no	Open
1218	6.185951942536062	-0.608307	-16.9528	0	19	18	0.86	0.00	-	no	Open
1220	6.302503376922587	-0.728794	-17.1543	1	18	16	0.76	0.00	-	yes	Open
1219	56.55356095897086	-0.842391	-19.2865	2	19	17	0.81	0.20	-	yes	Open
1221	57.284540487966105	-0.54862	-13.263	0	18	16	0.76	0.00	-	yes	Open
1223	58.227524812207875	-0.688666	-13.7569	1	20	16	0.76	0.00	-	yes	Open
1224	59.30284108553114	-0.647193	-8.96522	0	21	17	0.81	0.00	-	yes	Current
1217	60.186744343042065	-0.487181	-13.4669	0	18	15	0.71	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 -8.965kcal/mol

Ligand efficiency (LE) -0.2988kcal/mol/HA

Score / heavy atom count

Fit quality (FQ) -2.883

LE / (0.072 + 0.95/HAC) — Leeson & Springthorpe

Heavy atom count 30HA

Physicochemical properties

Molecular weight 404.6Da

Lipinski: ≤ 500 Da

LogP (cLogP) 4.11

Lipinski: ≤ 5

Rotatable bonds 4

Conformational strain (MMFF94s)

Strain energy (ΔE) 23.73kcal/mol

< 5 good · 5–10 marginal · > 10 problematic

Docked FF energy 74.44kcal/mol

Minimised FF energy 50.71kcal/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.

OSA_Lib_110