Protein target profile

KP13_00140

Zinc-type alcohol dehydrogenase-like protein

Genome: KpKP13 Gene: AHE42060.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H097

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Length 335

Pocket druggability 0.238

Direct ligand evidence 0 59 total records

Functional annotation 0 EC 5 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 (%): 34.239 Lower values reduce human off-target concern.
Human E-value: 3.45e-25
Gut microbiome similarity: 1.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.61 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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.

FPocket 0.238

Structure A0A0H3H097

Pocket Pocket 17

P2Rank 0.931

Structure A0A0H3H097

Pocket Pocket 1

ColabFold model

FPocket 0.906 · Pocket 3

P2Rank 0.93 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 91 / 4744 genomes with a hit

Prevalence 1.9%

Cross-references

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

Sequence

UniProt A0A0H3H097

Sequence

Primary amino-acid sequence viewer.

MKAIAITQAAADGNNIPSLTEIDLPIPTAHGRDLLVAVKAISVNPVDTKVRAGFQGDTPRVLGWDAVGVVQSVGEEVTLFAPGDEVWYAGALGRAGSNSEYQLVDERLVAHKPRTLDNASAAALPLTAITAWELLFHRLGVEEGGNAGDTLLIVGAAGGVGSILTQLASKLTAMTVIGTASRPESQQWVREAGAHHVIDHSKPLADELARIGITSVTHVASLTNTEQHFNALIDALAPQGKLALIDDPETLDVVPLKAKSLSLHWEFMFTRSMFETDDMIAQHQLLTRVAALIDNHTIKTTLGEHYGAITAANLQKAHRQLETGRAVGKIVLEGF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0008270 Binding to a zinc ion (Zn).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0003723 Binding to an RNA molecule or a portion thereof.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
14	332	SMART	SM00829	PKS_ER_names_mod
14	332	InterPro	IPR020843	Polyketide synthase, enoylreductase domain
33	89	Pfam	PF08240	Alcohol dehydrogenase GroES-like domain
33	89	InterPro	IPR013154	Alcohol dehydrogenase-like, N-terminal
148	169	ProSitePatterns	PS01162	Quinone oxidoreductase / zeta-crystallin signature.
148	169	InterPro	IPR002364	Quinone oxidoreductase/zeta-crystallin, conserved site
193	332	Pfam	PF13602	Zinc-binding dehydrogenase
25	332	Gene3D	G3DSA:3.90.180.10	-
127	274	Gene3D	G3DSA:3.40.50.720	-
1	333	PANTHER	PTHR44154	QUINONE OXIDOREDUCTASE
1	333	CDD	cd08252	AL_MDR
1	333	InterPro	IPR014182	Alcohol dehydrogenase, zinc-binding type 1
2	144	SUPERFAMILY	SSF50129	GroES-like
2	144	InterPro	IPR011032	GroES-like superfamily
116	286	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
116	286	InterPro	IPR036291	NAD(P)-binding domain superfamily
3	335	NCBIfam	TIGR02817	zinc-binding alcohol dehydrogenase family protein
3	335	InterPro	IPR014182	Alcohol dehydrogenase, zinc-binding type 1

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 · FPocket

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

Site 1 FPocket #17

0.238

Likely same site as P2Rank 1 1.2 Å 34 shared residues 89% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.931

Likely same site as FPocket 17 1.2 Å 34 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.037

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Surrounding area

Site 3 P2Rank #3

0.02

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.93

Likely same site as FPocket 3 0.5 Å 31 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.052

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Surrounding area

Site 3 P2Rank #3

0.015

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Surrounding area

Site 4 P2Rank #4

0.003

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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_A0A0H3H097	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00140	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1XX PDB via homolog 128.1 Da · LogP 0.76 · TPSA 46.5 Open detail RCSB PDB

2XX PDB via homolog Detail RCSB PDB

3XX PDB via homolog Detail RCSB PDB

4XX PDB via homolog Detail RCSB PDB

CO7 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
1XX RCSB PDB	4IDC	O23939	128.1 Da LogP 0.76 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@@H]1C(=O)C(=C(O1)C)O`
2XX RCSB PDB	4IDD	O23939	142.2 Da LogP 1.15 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@@H]1C(=O)C(=C(O1)C)O`
3XX RCSB PDB	4IDE	O23939	140.1 Da LogP 1.28 TPSA 46.5	✓ Ro5	✓ Clean	`C/C=C/1\C(=O)C(=C(O1)C)O`
4XX RCSB PDB	4IDF	O23939	114.1 Da LogP 0.38 TPSA 46.5	✓ Ro5	✓ Clean	`CC1=C(C(=O)CO1)O`
CO7 RCSB PDB	3B6Z	Q9Y7D0	835.6 Da LogP -0.76 TPSA 363.6	3 viol.	✓ Clean	`C/C=C/C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@…`
DIF RCSB PDB	2WEK	Q8N4Q0	296.2 Da LogP 4.36 TPSA 49.3	✓ Ro5	✓ Clean	`c1ccc(c(c1)CC(=O)O)Nc2c(cccc2Cl)Cl`
ETX RCSB PDB	1R37	P39462	90.1 Da LogP 0.02 TPSA 29.5	✓ Ro5	✓ Clean	`CCOCCO`
KZH RCSB PDB	5A3J	Q9SV68	292.4 Da LogP 4.84 TPSA 54.4	✓ Ro5	✓ Clean	`CCC=CCC(=O)C=CC=CCCCCCCCC(=O)O`
X1H RCSB PDB	2X1H	Q8N4Q0	376.4 Da LogP 5.22 TPSA 66.8	1 viol.	✓ Clean	`COc1ccc(cc1)C(=O)c2c3ccc(cc3sc2c4ccc(cc4)O)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
ZINC1281 ZINC	1.000	296.2 Da LogP 4.36 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC5650743 ZINC	0.875	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.875	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC2506700 ZINC	0.800	340.6 Da LogP 4.47 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Br`
ZINC26395789 ZINC	0.800	279.7 Da LogP 3.85 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(F)cccc1Cl`
ZINC33998501 ZINC	0.795	362.4 Da LogP 4.92 TPSA 77.8	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1)c1c(-c2ccc(O)cc2)sc2cc(O)ccc12`
ZINC2383046 ZINC	0.743	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cc(O)cc1Cl`
ZINC3805798 ZINC	0.737	354.2 Da LogP 3.91 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC13558626 ZINC	0.722	310.2 Da LogP 4.45 TPSA 38.3	✓ Ro5	✓ Clean	`COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC39330321 ZINC	0.703	323.2 Da LogP 4.37 TPSA 32.3	✓ Ro5	✓ Clean	`CN(C)C(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC6095281 ZINC	0.703	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)ccc(O)c1Cl`
ZINC44699349 ZINC	0.700	412.2 Da LogP 3.45 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)COC(=O)COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC44699432 ZINC	0.700	470.3 Da LogP 2.99 TPSA 128.2	✓ Ro5	✓ Clean	`O=C(O)COC(=O)COC(=O)COC(=O)Cc1ccccc1Nc1c(Cl)ccc…`
ZINC2506699 ZINC	0.697	268.1 Da LogP 4.23 TPSA 32.3	✓ Ro5	✓ Clean	`OCc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC22060327 ZINC	0.694	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1cc(O)ccc1Nc1c(Cl)cccc1Cl`
ZINC44699442 ZINC	0.667	324.2 Da LogP 4.84 TPSA 38.3	✓ Ro5	✓ Clean	`CCOC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC34537110 ZINC	0.660	447.5 Da LogP 4.73 TPSA 95.9	✓ Ro5	✓ Clean	`CC(=O)NCCOc1ccc(C(=O)c2c(-c3ccc(O)cc3)sc3cc(O)c…`
ZINC2060993406 ZINC	0.651	398.2 Da LogP 3.92 TPSA 84.9	✓ Ro5	✓ Clean	`O=C(O)COCCOC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC1346 ZINC	0.649	302.2 Da LogP 4.43 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1cscc1Nc1c(Cl)cccc1Cl`
ZINC2060993414 ZINC	0.643	368.2 Da LogP 4.30 TPSA 75.6	✓ Ro5	✓ Clean	`C[C@H](OC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl)C(=O)O`
ZINC71404741 ZINC	0.641	292.4 Da LogP 4.84 TPSA 54.4	✓ Ro5	✓ Clean	`CC/C=C\C/C=C\C=C\C(=O)CCCCCCCC(=O)O`
ZINC1775964273 ZINC	0.639	224.3 Da LogP 3.11 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)/C=C/C=C/CCCCCCC(=O)O`
ZINC2325860610 ZINC	0.634	395.3 Da LogP 3.28 TPSA 81.6	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1Nc1c(Cl)cccc1Cl)N[C@H]1C[C@H](O)[C…`
ZINC38600110 ZINC	0.634	368.2 Da LogP 4.00 TPSA 64.6	✓ Ro5	✓ Clean	`COC(=O)COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC2569322 ZINC	0.629	282.1 Da LogP 4.44 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1c(Cl)cccc1Cl`
ZINC403523 ZINC	0.606	227.3 Da LogP 3.06 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1ccccc1`
ZINC2297732054 ZINC	0.595	294.4 Da LogP 4.63 TPSA 57.5	✓ Ro5	✓ Clean	`CCC=CC[C@H](O)C=CC=CCCCCCCCC(=O)O`
ZINC2333257289 ZINC	0.595	294.4 Da LogP 4.63 TPSA 57.5	✓ Ro5	✓ Clean	`CCC=CC[C@@H](O)C=CC=CCCCCCCCC(=O)O`
ZINC34961834 ZINC	0.595	294.4 Da LogP 4.63 TPSA 57.5	✓ Ro5	✓ Clean	`CC/C=C\C[C@H](O)/C=C/C=C\CCCCCCCC(=O)O`
ZINC83314730 ZINC	0.595	266.4 Da LogP 3.85 TPSA 57.5	✓ Ro5	✓ Clean	`CC/C=C\C[C@H](O)/C=C/C=C\CCCCCC(=O)O`
ZINC33822120 ZINC	0.595	250.4 Da LogP 4.88 TPSA 37.3	✓ Ro5	✓ Clean	`CC/C=C\C/C=C\C/C=C\CCCCCC(=O)O`
ZINC2060993409 ZINC	0.587	440.3 Da LogP 4.23 TPSA 101.9	✓ Ro5	✓ Clean	`C[C@H](OC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl)C(=O)O[C@…`
ZINC2060993410 ZINC	0.587	440.3 Da LogP 4.23 TPSA 101.9	✓ Ro5	✓ Clean	`C[C@H](OC(=O)[C@@H](C)OC(=O)Cc1ccccc1Nc1c(Cl)cc…`
ZINC2060993411 ZINC	0.587	440.3 Da LogP 4.23 TPSA 101.9	✓ Ro5	✓ Clean	`C[C@H](OC(=O)[C@H](C)OC(=O)Cc1ccccc1Nc1c(Cl)ccc…`
ZINC2060993412 ZINC	0.587	440.3 Da LogP 4.23 TPSA 101.9	✓ Ro5	✓ Clean	`C[C@@H](OC(=O)[C@@H](C)OC(=O)Cc1ccccc1Nc1c(Cl)c…`
ZINC65742970 ZINC	0.575	310.4 Da LogP 4.04 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)/C=C/C=C\CCCCCCCCCO`
ZINC584906798 ZINC	0.565	393.3 Da LogP 4.92 TPSA 41.6	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1Nc1c(Cl)cccc1Cl)OCCN1CCCC1`
ZINC12501520 ZINC	0.563	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC2386141 ZINC	0.563	205.0 Da LogP 2.62 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1cccc(Cl)c1Cl`
ZINC3874716 ZINC	0.563	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	0.563	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.563	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	0.563	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.563	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5859031 ZINC	0.563	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC117698057 ZINC	0.558	310.4 Da LogP 4.03 TPSA 74.6	✓ Ro5	✓ Clean	`CC/C=C\C[C@H](O)C(=O)C/C=C\CCCCCCCC(=O)O`
ZINC43898792 ZINC	0.553	334.5 Da LogP 4.37 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCC/C=C\CC(=O)/C=C\C=C/C=C/[C@@H](O)CCCC(=O)O`
ZINC4632131 ZINC	0.553	334.5 Da LogP 4.37 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCC/C=C\CC(=O)/C=C/C=C/C=C\[C@@H](O)CCCC(=O)O`
ZINC256051021 ZINC	0.550	297.1 Da LogP 3.76 TPSA 62.2	✓ Ro5	✓ Clean	`O=C(O)Cc1cccc(Nc2c(Cl)cccc2Cl)n1`
ZINC396292 ZINC	0.550	228.2 Da LogP 2.63 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(C(=O)c2ccc(O)cc2)cc1`

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.

KP13_00140

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Sequence

Functional annotations

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence