Protein target profile

KP13_03500

Protein moaE

Genome: KpKP13 Gene: AHE45876.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GPH4

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Length 254

Pocket druggability 0.043

Direct ligand evidence 0 59 total records

Functional annotation 0 EC 1 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 (%): 39.785 Lower values reduce human off-target concern.
Human E-value: 5.7e-11
Gut microbiome similarity: 0.3% 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: 97.37 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 0.043

Structure A0A0H3GPH4

Pocket Pocket 2

P2Rank 0.932

Structure A0A0H3GPH4

Pocket Pocket 1

ColabFold model

FPocket 0.268 · Pocket 19

P2Rank 0.947 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 14 / 4744 genomes with a hit

Prevalence 0.3%

Cross-references

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

Sequence

UniProt A0A0H3GPH4

Sequence

Primary amino-acid sequence viewer.

MVITGGGTGIGAACARLMRAAGDRVFITGRREAPLQAVANETGATALVGDAADGEVWRQRLLPAILDQTGGIDVLICSAGGMGNSPAAETSDRQWREALDGNLTSAFASVRACLPSLIARRGNVLFVASIASLAAGPQACGYVTAKHALIGLMRSVARDYGPQGVRANAICPGWVTTPMADEEMHPLMQAEGLSLTEAYQRVCRDVPLRRPASPEEIAEACQFLCSPQAAIISGATLVADGGASIVDVPTLAFA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
142	161	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
142	161	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
163	180	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
163	180	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
70	81	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
70	81	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
38	55	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
38	55	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
207	227	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
207	227	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
116	132	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
116	132	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
2	246	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	246	InterPro	IPR036291	NAD(P)-binding domain superfamily
2	177	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
129	157	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
129	157	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
142	161	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
70	81	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
122	130	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
122	130	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
14	240	CDD	cd05233	SDR_c
1	249	Gene3D	G3DSA:3.40.50.720	-
1	248	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
2	244	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
8	243	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase

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

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

Site 1 P2Rank #1

0.932

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Surrounding area

Site 2 P2Rank #2

0.485

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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

0.947

Likely same site as FPocket 19 7.0 Å 19 shared residues 76% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.089

Likely same site as FPocket 19 7.3 Å 2 shared residues 33% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.004

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Surrounding area

Site 4 P2Rank #4

0.004

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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_A0A0H3GPH4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03500	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

3HR PDB via homolog 104.1 Da · LogP -0.16 · TPSA 57.5 Open detail RCSB PDB

A6O PDB via homolog Detail RCSB PDB

AAE PDB via homolog Detail RCSB PDB

DXX PDB via homolog Detail RCSB PDB

EMO 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
3HR RCSB PDB	3VDR	D0VWQ0	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)O`
A6O RCSB PDB	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
AAE RCSB PDB	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
DXX RCSB PDB	3W8D	D0VWQ0	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
EMO RCSB PDB	2RH4	P16544	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc2c(c(c1)O)C(=O)c3c(cc(cc3O)O)C2=O`
ISZ RCSB PDB	1XR3	P16544	135.1 Da LogP 1.25 TPSA 66.2	✓ Ro5	Alert	`[H]/N=N/C(=O)c1ccncc1`
MLA RCSB PDB	3W8F	D0VWQ0	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
QT8 RCSB PDB	6ZZS	A0A1E3M3N6	116.1 Da LogP 0.44 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)CC(=O)O`
TAM RCSB PDB	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
ZINC3824868 ZINC	1.000	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC4095655 ZINC	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3978794 ZINC	0.697	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)c2c(c1)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC3861630 ZINC	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC1845623 ZINC	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2\CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC1845624 ZINC	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2/CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC14760847 ZINC	0.667	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC5277130 ZINC	0.656	238.2 Da LogP 2.48 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1ccccc1C2=O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC4098655 ZINC	0.629	304.7 Da LogP 2.54 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(Cl)c(O)c1C2=O`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC2575038 ZINC	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC5461939 ZINC	0.618	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1O)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14814143 ZINC	0.595	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1c(O)ccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13481200 ZINC	0.594	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)cc(O)cc21`
ZINC3977762 ZINC	0.588	300.2 Da LogP 1.28 TPSA 132.1	✓ Ro5	Alert	`O=C(O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC5812872 ZINC	0.588	286.2 Da LogP 1.07 TPSA 115.1	✓ Ro5	Alert	`O=C1c2cc(O)cc(O)c2C(=O)c2c(O)cc(CO)cc21`
ZINC6070245 ZINC	0.588	256.3 Da LogP 2.25 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)Cc1cc(O)cc(O)c1C2=O`
ZINC14760863 ZINC	0.579	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1c(O)c(C)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC6070262 ZINC	0.579	314.2 Da LogP 1.59 TPSA 132.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1C(=O)O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC14819806 ZINC	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14819808 ZINC	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC31163880 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc…`
ZINC31163884 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163888 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163892 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O…`
ZINC13334425 ZINC	0.564	268.3 Da LogP 2.48 TPSA 63.6	✓ Ro5	Alert	`COc1cccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13546016 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC13546018 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC257400894 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC257400895 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC14760819 ZINC	0.553	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1cc(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC5412537 ZINC	0.553	316.3 Da LogP 1.60 TPSA 124.3	✓ Ro5	Alert	`COc1c(O)c(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC20111521 ZINC	0.550	327.3 Da LogP 1.95 TPSA 98.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(CN(C)C)c(O)c1C2=O`
ZINC1662285 ZINC	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C\CC1(C)C(=O)CCC1=O`
ZINC17380200 ZINC	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C/CC1(C)C(=O)CCC1=O`
ZINC77257242 ZINC	0.538	316.3 Da LogP 1.43 TPSA 124.3	✓ Ro5	Alert	`COCc1c(O)cc2c(c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC1637808 ZINC	0.528	267.1 Da LogP 2.36 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)C=C(Br)C2=O`
ZINC13398014 ZINC	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC14811261 ZINC	0.512	300.3 Da LogP 1.37 TPSA 104.1	✓ Ro5	Alert	`COc1cc(CO)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC4098672 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](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.

KP13_03500

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 · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence