KpKP13 Protein target profile

50S ribosomal protein L13

Accession: KP13_03996

Gene: rplM AHE42452.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GW96

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Length 142

Pocket druggability (P2Rank · AlphaFold DB model) 0.055

Direct ligand evidence 0 55 total records

Functional annotation 0 EC 6 GO

Target summary

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.

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: Hit
Human identity (%): 37.0 Lower values reduce human off-target concern.
Human E-value: 1.84e-19
Gut microbiome similarity: 63.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.479 Higher values support similarity to known essential genes.
DEG E-value: 4.06e-101 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.29 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.055

Structure A0A0H3GW96

Pocket Pocket 1

Druggability (FPocket) 0.338

Structure A0A0H3GW96

Pocket Pocket 4

ColabFold model

P2Rank 0.021 · Pocket 1

FPocket 0.5 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3000 / 4744 genomes with a hit

Prevalence 63.2%

Sequence

Primary amino-acid sequence viewer.

MKTFTAKPETVKRDWYVVDATGKTLGRLATELARRLRGKHKAEYTPHVDTGDYIIVLNAEKVAVTGNKREDKMYYHHTGHIGGIKEATFEEMIARRPERVIEIAVKGMLPKGPLGRAMYRKLKVYAGNEHNHAAQQPQVLDI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:0022625 The large subunit of a ribosome located in the cytosol.
GO:0003729 Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
GO:0017148 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
1	142	PIRSF	PIRSF002181	RPL13p_RPL13Aa_RPL16e_RPL13o
1	142	InterPro	IPR005822	Ribosomal protein L13
4	142	NCBIfam	TIGR01066	50S ribosomal protein L13
4	142	InterPro	IPR005823	Ribosomal protein L13, bacterial-type
15	128	CDD	cd00392	Ribosomal_L13
15	128	InterPro	IPR005822	Ribosomal protein L13
105	127	ProSitePatterns	PS00783	Ribosomal protein L13 signature.
105	127	InterPro	IPR023563	Ribosomal protein L13, conserved site
1	141	PANTHER	PTHR11545	RIBOSOMAL PROTEIN L13
1	141	InterPro	IPR005822	Ribosomal protein L13
13	131	Pfam	PF00572	Ribosomal protein L13
13	131	InterPro	IPR005822	Ribosomal protein L13
1	142	FunFam	G3DSA:3.90.1180.10:FF:000001	50S ribosomal protein L13
1	142	Gene3D	G3DSA:3.90.1180.10	Ribosomal protein L13
1	142	InterPro	IPR036899	Ribosomal protein L13 superfamily
1	140	SUPERFAMILY	SSF52161	Ribosomal protein L13
1	140	InterPro	IPR036899	Ribosomal protein L13 superfamily
15	141	Hamap	MF_01366	50S ribosomal protein L13 [rplM].
15	141	InterPro	IPR005822	Ribosomal protein L13

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.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.055

Likely same site as FPocket 4 1.5 Å 10 shared residues 91% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #4

0.338

Likely same site as P2Rank 1 1.5 Å 10 shared residues 91% of smaller site

Show in viewer

Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental 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 AF_A0A0H3GW96	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03996	ColabFold	—	—	full sequence	—	Loaded

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.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

NMY PDB via homolog 614.7 Da · LogP -8.90 · TPSA 353.1 Open detail RCSB PDB

OHX PDB via homolog Detail RCSB PDB

PAR PDB via homolog Detail RCSB PDB

SPD PDB via homolog Detail RCSB PDB

YMZ PDB via homolog Detail RCSB PDB

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
NMY RCSB PDB	4V9C	P0AA10	614.7 Da LogP -8.90 TPSA 353.1	3 viol.	✓ Clean	`C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…`
OHX RCSB PDB	4V8E	P60488	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`
PAR RCSB PDB	4WOI	P0AA10	615.6 Da LogP -8.86 TPSA 347.3	3 viol.	✓ Clean	`C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…`
SPD RCSB PDB	5JVG	Q9RXY1	145.2 Da LogP -0.34 TPSA 64.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CN`
YMZ RCSB PDB	5UMD	Q8IJZ7	378.3 Da LogP 4.45 TPSA 45.2	✓ Ro5	✓ Clean	`c1cc2c(cc(nc2c(c1)C(F)(F)F)C(F)(F)F)[C@H]([C@@H…`

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
ZINC3874185 ZINC	1.000	378.3 Da LogP 4.45 TPSA 45.2	✓ Ro5	✓ Clean	`O[C@@H](c1cc(C(F)(F)F)nc2c(C(F)(F)F)cccc12)[C@@…`
ZINC27564039 ZINC	0.933	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742 ZINC	0.929	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC1532734 ZINC	0.929	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC100052153 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC100223147 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](…`
ZINC103649633 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC242575106 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575107 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575108 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575109 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC43664294 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664297 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664300 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664303 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC53255716 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC56874669 ZINC	0.881	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC1598087 ZINC	0.867	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC60184027 ZINC	0.786	455.5 Da LogP -6.62 TPSA 256.6	2 viol.	✓ Clean	`N[C@H]1C[C@@H](N)[C@H](O)[C@@H](O[C@@H]2O[C@H](…`
ZINC256001609 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC256001610 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC256001611 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC256001612 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC53132258 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC77301567 ZINC	0.717	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@H]2[C@H](N)C[C@H](N)[C@@H](O…`
ZINC1568067 ZINC	0.714	392.3 Da LogP 4.84 TPSA 45.1	✓ Ro5	✓ Clean	`O[C@H](C[C@H]1CCCCN1)c1cc(C(F)(F)F)nc2c(C(F)(F)…`
ZINC1568068 ZINC	0.714	392.3 Da LogP 4.84 TPSA 45.1	✓ Ro5	✓ Clean	`O[C@@H](C[C@H]1CCCCN1)c1cc(C(F)(F)F)nc2c(C(F)(F…`
ZINC1568069 ZINC	0.714	392.3 Da LogP 4.84 TPSA 45.1	✓ Ro5	✓ Clean	`O[C@H](C[C@@H]1CCCCN1)c1cc(C(F)(F)F)nc2c(C(F)(F…`
ZINC1568070 ZINC	0.714	392.3 Da LogP 4.84 TPSA 45.1	✓ Ro5	✓ Clean	`O[C@@H](C[C@@H]1CCCCN1)c1cc(C(F)(F)F)nc2c(C(F)(…`
ZINC245224241 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O)[C@@H]…`
ZINC245224242 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O)[C@@H]…`
ZINC245224243 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O)[C@@H]…`
ZINC255189913 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC4095654 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC45076909 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC45076911 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@@H](N)[C@H]…`
ZINC59846619 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O)[C@@H]…`
ZINC59846620 ZINC	0.698	322.4 Da LogP -5.12 TPSA 203.5	1 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O)[C@H](…`
ZINC100056474 ZINC	0.650	270.5 Da LogP 4.63 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNCCCN`
ZINC107767463 ZINC	0.650	200.4 Da LogP 2.68 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCNCCCCCCN`
ZINC59496006 ZINC	0.650	242.5 Da LogP 3.85 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNCCCN`
ZINC1572960 ZINC	0.643	379.2 Da LogP 4.74 TPSA 45.2	✓ Ro5	✓ Clean	`O[C@@H](c1cc(C(F)(F)F)nc2c(Cl)cc(Cl)cc12)[C@H]1…`
ZINC1572961 ZINC	0.643	379.2 Da LogP 4.74 TPSA 45.2	✓ Ro5	✓ Clean	`O[C@H](c1cc(C(F)(F)F)nc2c(Cl)cc(Cl)cc12)[C@H]1C…`
ZINC1572962 ZINC	0.643	379.2 Da LogP 4.74 TPSA 45.2	✓ Ro5	✓ Clean	`O[C@@H](c1cc(C(F)(F)F)nc2c(Cl)cc(Cl)cc12)[C@@H]…`
ZINC1572963 ZINC	0.643	379.2 Da LogP 4.74 TPSA 45.2	✓ Ro5	✓ Clean	`O[C@H](c1cc(C(F)(F)F)nc2c(Cl)cc(Cl)cc12)[C@@H]1…`
ZINC239203290 ZINC	0.625	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O[C@@H]3…`
ZINC242649355 ZINC	0.625	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC242649358 ZINC	0.625	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC8101132 ZINC	0.625	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O[C@H]3O…`
ZINC8217403 ZINC	0.625	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GW96

50S ribosomal protein L13

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence