Protein target profile
HT085_RS00370
signal peptidase II
Target candidate with partial support; inspect missing evidence before prioritizing.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
Terms and data sources used on this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Prioritization evidence
Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.
Off-target risk
- Human off-target
- No hit
- Gut microbiome off-target
- Hit
Essentiality
- Essential (DEG)
- Y
Localization
- Localization
- CytoplasmicMembrane
Binding-site evidence
The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MSSSVSSKTRYWVLALAAIVLDQWSKWAVLSSFQYRERVNVIPSFFDLTLVYNPGAAFSFLADQGGWQKYFFLVLAVAVSAYLVRAILRDEFAALGKIGAAMIIGGASGNVIDRLIHGHVVDFLLFYWQNWFYPAFNIADSFICVGAVLAVLDNIVHRKDSKKT
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
3- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0004190 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 130 | 152 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 15 | 153 | Pfam | PF01252 | Signal peptidase (SPase) II |
| 15 | 153 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 1 | 11 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 12 | 29 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 41 | 61 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 93 | 115 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 92 | 112 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 7 | 161 | Hamap | MF_00161 | Lipoprotein signal peptidase [lspA]. |
| 7 | 161 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 132 | 152 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 100 | 115 | PRINTS | PR00781 | Lipoprotein signal peptidase family (A8) signature |
| 100 | 115 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 136 | 152 | PRINTS | PR00781 | Lipoprotein signal peptidase family (A8) signature |
| 136 | 152 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 53 | 61 | PRINTS | PR00781 | Lipoprotein signal peptidase family (A8) signature |
| 53 | 61 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 39 | 61 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 113 | 131 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 62 | 66 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 8 | 163 | NCBIfam | TIGR00077 | signal peptidase II |
| 8 | 163 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 153 | 164 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 30 | 40 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 71 | 88 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 8 | 162 | PANTHER | PTHR33695 | LIPOPROTEIN SIGNAL PEPTIDASE |
| 8 | 162 | InterPro | IPR001872 | Peptidase A8, signal peptidase II |
| 86 | 91 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 67 | 85 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
3D structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
How colors and pocket overlays are used
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
All structural evidence
Structural evidence
0 + 1Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
HT085_RS00370
|
AlphaFold DB | — | — | full sequence | — | Viewing |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Structural ligand evidence is available for this target.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| 7PE RCSB PDB | Q6GHN9 | 310.4 Da LogP 0.10 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCOCCOCCO
|
|
| KNH RCSB PDB | Q6GHN9 | 623.9 Da LogP 5.20 TPSA 142.4 | 2 viol. | ✓ Clean |
CCC[C@H]1C(=O)NC[C@H](C[C@@H]([C@@H](CC/C(=C/C=…
|
|
| OLC RCSB PDB | Q6GHN9 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)O
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC1501016272 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO
|
| ZINC1501016273 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC1501016315 ZINC | 1.000 | 314.5 Da LogP 3.75 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC1501016316 ZINC | 1.000 | 314.5 Da LogP 3.75 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO
|
| ZINC2038077522 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC=CCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC2038077523 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC=CCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC221534416 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)CO
|
| ZINC32840893 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC32840894 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC32840895 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC32840896 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC32840901 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC32840902 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC32840903 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC32840904 ZINC | 1.000 | 356.5 Da LogP 4.92 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC5650743 ZINC | 1.000 | 222.3 Da LogP 0.07 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCO
|
| ZINC6403917 ZINC | 1.000 | 354.4 Da LogP 0.11 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC725433050 ZINC | 1.000 | 342.5 Da LogP 4.53 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC725433052 ZINC | 1.000 | 342.5 Da LogP 4.53 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO
|
| ZINC98208566 ZINC | 1.000 | 328.5 Da LogP 4.14 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO
|
| ZINC32840885 ZINC | 0.943 | 300.4 Da LogP 3.36 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC2053467566 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC=CCC=CCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC2053467567 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCC=CCC=CCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC29045599 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C/C/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC4557100 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC4557101 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC5819989 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC5819990 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC85425978 ZINC | 0.919 | 354.5 Da LogP 4.70 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C\C/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC29045446 ZINC | 0.892 | 352.5 Da LogP 4.47 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)OC[C@@H](O)CO
|
| ZINC13532428 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC13532431 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC13532435 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC13546140 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC13546141 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC2296552808 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC2296552809 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC33832849 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC35052109 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC4411072 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC4411074 ZINC | 0.829 | 372.5 Da LogP 3.89 TPSA 87.0 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC100297583 ZINC | 0.824 | 232.3 Da LogP 1.63 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC100503477 ZINC | 0.824 | 260.4 Da LogP 2.41 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC100503478 ZINC | 0.824 | 260.4 Da LogP 2.41 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC2516268 ZINC | 0.824 | 218.3 Da LogP 1.24 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC2568190 ZINC | 0.824 | 232.3 Da LogP 1.63 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC38153421 ZINC | 0.824 | 246.3 Da LogP 2.02 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC(=O)OC[C@@H](O)CO
|
| ZINC8437476 ZINC | 0.824 | 274.4 Da LogP 2.80 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC95669489 ZINC | 0.824 | 288.4 Da LogP 3.19 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC(=O)OC[C@H](O)CO
|
| ZINC95669491 ZINC | 0.824 | 288.4 Da LogP 3.19 TPSA 66.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC(=O)OC[C@@H](O)CO
|
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.