Protein target profile

KP13_01290

Aspartate carbamoyltransferase

Genome: KpKP13 Gene: AHE46644.1 pyrB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GMI1

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Length 311

Pocket druggability 0.074

Direct ligand evidence 0 70 total records

Functional annotation 1 EC 7 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 (%): 42.345 Lower values reduce human off-target concern.
Human E-value: 1.23e-74
Gut microbiome similarity: 13.0% 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: 95.41 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 0.074

Structure A0A0H3GMI1

Pocket Pocket 6

P2Rank 0.532

Structure A0A0H3GMI1

Pocket Pocket 1

ColabFold model

FPocket 0.875 · Pocket 5

P2Rank 0.622 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 616 / 4744 genomes with a hit

Prevalence 13.0%

Cross-references

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

Sequence

UniProt A0A0H3GMI1

Chemistry

ChEMBL CHEMBL170214 ChEMBL CHEMBL29908

Sequence

Primary amino-acid sequence viewer.

MANPLYQKHIISINDLSREDLELVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGGVPVLNAGDGANQHPTQTLLDLFTIQETQGRLENLNVAMVGDLKYGRTVHSLTQALAKFNGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSAIDDVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRAADLEGARANMKVLHPLPRIDEITTDVDKTPHAWYFQQAGNGIFARQALLALVLNSELAL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.1.3.2

Gene Ontology (GO)

GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
GO:0016597 Binding to an amino acid, organic acids containing one or more amino substituents.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0004070 Catalysis of the reaction: L-aspartate + carbamoyl phosphate = N-carbamoyl-L-aspartate + H+ + phosphate.
GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
9	302	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
9	302	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
135	292	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
135	292	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
138	292	FunFam	G3DSA:3.40.50.1370:FF:000002	Aspartate carbamoyltransferase 2
7	307	Hamap	MF_00001	Aspartate carbamoyltransferase [pyrB].
7	307	InterPro	IPR002082	Aspartate carbamoyltransferase
3	307	PANTHER	PTHR45753	ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
4	306	SUPERFAMILY	SSF53671	Aspartate/ornithine carbamoyltransferase
4	306	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
9	137	FunFam	G3DSA:3.40.50.1370:FF:000001	Aspartate carbamoyltransferase
8	305	NCBIfam	TIGR00670	aspartate carbamoyltransferase
8	305	InterPro	IPR002082	Aspartate carbamoyltransferase
39	61	PRINTS	PR00101	Aspartate carbamoyltransferase signature
79	88	PRINTS	PR00101	Aspartate carbamoyltransferase signature
226	235	PRINTS	PR00101	Aspartate carbamoyltransferase signature
134	151	PRINTS	PR00101	Aspartate carbamoyltransferase signature
286	300	PRINTS	PR00101	Aspartate carbamoyltransferase signature
264	269	PRINTS	PR00101	Aspartate carbamoyltransferase signature
49	56	ProSitePatterns	PS00097	Aspartate and ornithine carbamoyltransferases signature.
49	56	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
8	148	Pfam	PF02729	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
8	148	InterPro	IPR006132	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
270	293	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
270	293	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
49	68	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
49	68	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
260	269	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
260	269	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
135	146	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
135	146	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
155	303	Pfam	PF00185	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
155	303	InterPro	IPR006131	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain

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

0.532

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Surrounding area

Site 2 P2Rank #2

0.099

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Surrounding area

Residue sets

UniProt: Binding site:106-106

UniProt: Binding site:135-135

UniProt: Binding site:138-138

UniProt: Binding site:168-168

UniProt: Binding site:230-230

UniProt: Binding site:268-268

UniProt: Binding site:269-269

UniProt: Binding site:55-55

UniProt: Binding site:56-56

UniProt: Binding site:85-85

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.622

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.049

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Surrounding area

Site 3 P2Rank #3

0.039

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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_A0A0H3GMI1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01290	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.

70 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1IP PDB via homolog 254.1 Da · LogP -2.39 · TPSA 167.0 Open detail RCSB PDB

6PR PDB via homolog Detail RCSB PDB

AL0 PDB via homolog Detail RCSB PDB

CP PDB via homolog Detail RCSB PDB

D48 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
1IP RCSB PDB	2IPO	P0A786	254.1 Da LogP -2.39 TPSA 167.0	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)NC(=O)CP(=O)(O)O)C(=O)N`
6PR RCSB PDB	2H3E	P0A786	254.1 Da LogP -2.39 TPSA 167.0	✓ Ro5	✓ Clean	`C([C@@H](C(=O)N)NC(=O)CP(=O)(O)O)C(=O)O`
AL0 RCSB PDB	2AIR	P0A786	149.1 Da LogP -1.23 TPSA 116.2	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)N(N=O)O`
CP RCSB PDB	1ZA2	P0A786	141.0 Da LogP -0.83 TPSA 109.9	✓ Ro5	✓ Clean	`C(=O)(N)OP(=O)(O)O`
D48 RCSB PDB	6FBA	O15804	160.2 Da LogP 2.25 TPSA 40.5	✓ Ro5	Alert	`c1ccc2cc(c(cc2c1)O)O`
DOR RCSB PDB	4C6K	P27708	158.1 Da LogP -1.33 TPSA 95.5	✓ Ro5	✓ Clean	`C1[C@H](NC(=O)NC1=O)C(=O)O`
EOB RCSB PDB	2FZG	P0A786	352.2 Da LogP -0.08 TPSA 173.3	1 viol.	✓ Clean	`c1cc(cc(c1)NC(=O)CP(=O)(O)O)NC(=O)CP(=O)(O)O`
EOP RCSB PDB	2FZC	P0A786	304.1 Da LogP -2.43 TPSA 173.3	1 viol.	✓ Clean	`C(CNC(=O)CP(=O)(O)O)NC(=O)CP(=O)(O)O`
EOZ RCSB PDB	2FZK	P0A786	396.2 Da LogP -0.38 TPSA 210.6	1 viol.	✓ Clean	`c1c(cc(cc1NC(=O)CP(=O)(O)O)NC(=O)CP(=O)(O)O)C(=…`
FLC RCSB PDB	1R0B	P0A786	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
FOT RCSB PDB	4C6L	P27708	174.1 Da LogP -1.10 TPSA 103.0	✓ Ro5	✓ Clean	`C1(=C(NC(=O)NC1=O)C(=O)O)F`
MAE RCSB PDB	2IPO	P0A786	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)/C(=O)O`
MLI RCSB PDB	1AT1	P0A786	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT RCSB PDB	1NBE	P0A786	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NCD RCSB PDB	1R0C	P0A786	176.1 Da LogP -1.42 TPSA 129.7	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)NC(=O)N)C(=O)O`
ORO RCSB PDB	4C6Q	P27708	156.1 Da LogP -1.24 TPSA 103.0	✓ Ro5	✓ Clean	`C1=C(NC(=O)NC1=O)C(=O)O`
PAL RCSB PDB	1ACM	P0A786	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)NC(=O)CP(=O)(O)O)C(=O)O`
PCT RCSB PDB	1AT1	P0A786	139.0 Da LogP -1.35 TPSA 100.6	✓ Ro5	✓ Clean	`C(C(=O)N)P(=O)(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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL170214 ChEMBL	P27708	6.85 ~141.3 nM	188.2 Da LogP -0.08 TPSA 78.8	✓ Ro5	✓ Clean	`O=C1N=C(CS)CC(C(=O)O)N1`
CHEMBL29908 ChEMBL	P27708	6.85 ~141.3 nM	190.2 Da LogP -0.56 TPSA 78.4	✓ Ro5	✓ Clean	`O=C1N[C@@H](CS)C[C@@H](C(=O)O)N1`

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
ZINC1563934 ZINC	1.000	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)CP(=O)(O)O)C(=O)O`
ZINC1756826 ZINC	1.000	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)CP(=O)(O)O)C(=O)O`
ZINC71773889 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC1998878 ZINC	0.650	223.1 Da LogP 3.31 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1cc2ccccc2cc1Br`
ZINC71256830 ZINC	0.650	270.1 Da LogP 3.15 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1cc2ccccc2cc1I`
ZINC1865661 ZINC	0.629	283.2 Da LogP -0.75 TPSA 150.2	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)CC(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1865662 ZINC	0.629	283.2 Da LogP -0.75 TPSA 150.2	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)CC(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC71256619 ZINC	0.619	220.3 Da LogP 4.21 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1cc2ccccc2cc1-c1ccccc1`
ZINC5131744 ZINC	0.609	249.2 Da LogP -1.57 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131745 ZINC	0.609	249.2 Da LogP -1.57 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131908 ZINC	0.609	249.2 Da LogP -1.57 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC469834 ZINC	0.606	264.3 Da LogP 2.08 TPSA 95.5	✓ Ro5	✓ Clean	`CCC(=O)Nc1cc(NC(=O)CC)cc(C(=O)O)c1`
ZINC1709621 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709622 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709623 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709624 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1575288 ZINC	0.593	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575289 ZINC	0.593	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575290 ZINC	0.593	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC1575291 ZINC	0.593	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC1642634 ZINC	0.593	200.1 Da LogP -1.54 TPSA 140.3	✓ Ro5	✓ Clean	`O=C(O)c1[nH]c(=O)[nH]c(=O)c1C(=O)O`
ZINC22150060 ZINC	0.588	216.2 Da LogP -0.52 TPSA 109.5	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@@H](CC(N)=O)C(=O)O`
ZINC22150064 ZINC	0.588	216.2 Da LogP -0.52 TPSA 109.5	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@H](CC(N)=O)C(=O)O`
ZINC3107243 ZINC	0.588	352.3 Da LogP 0.99 TPSA 170.1	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)Nc1cc(NC(=O)CCC(=O)O)cc(C(=O)O)c1`
ZINC32594169 ZINC	0.581	222.2 Da LogP -0.52 TPSA 110.2	✓ Ro5	✓ Clean	`NCC(=O)Nc1cccc(NC(=O)CN)c1`
ZINC5307402 ZINC	0.581	220.3 Da LogP 2.38 TPSA 58.2	✓ Ro5	✓ Clean	`CCC(=O)Nc1cccc(NC(=O)CC)c1`
ZINC1642475 ZINC	0.571	282.0 Da LogP -0.63 TPSA 103.0	✓ Ro5	✓ Clean	`O=C(O)c1[nH]c(=O)[nH]c(=O)c1I`
ZINC1666478 ZINC	0.571	235.0 Da LogP -0.48 TPSA 103.0	✓ Ro5	✓ Clean	`O=C(O)c1[nH]c(=O)[nH]c(=O)c1Br`
ZINC1731782 ZINC	0.571	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1731783 ZINC	0.571	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1731784 ZINC	0.571	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC1731785 ZINC	0.571	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC39204122 ZINC	0.565	200.3 Da LogP 3.84 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)(C)c1cc2ccccc2cc1O`
ZINC1583347 ZINC	0.563	276.3 Da LogP 1.52 TPSA 92.3	✓ Ro5	✓ Clean	`CC(=O)CC(=O)Nc1cccc(NC(=O)CC(C)=O)c1`
ZINC969509 ZINC	0.563	213.1 Da LogP -2.12 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1cc(=O)[nH]c(=O)[nH]1`
ZINC22040791 ZINC	0.560	292.2 Da LogP -1.98 TPSA 173.3	1 viol.	✓ Clean	`O=C(O)C[C@H](NCCN[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC22589819 ZINC	0.560	292.2 Da LogP -1.98 TPSA 173.3	1 viol.	✓ Clean	`O=C(O)C[C@@H](NCCN[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC23377883 ZINC	0.560	292.2 Da LogP -1.98 TPSA 173.3	1 viol.	✓ Clean	`O=C(O)C[C@H](NCCN[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131760 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131761 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131922 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131923 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC11638239 ZINC	0.559	237.2 Da LogP 1.43 TPSA 103.7	✓ Ro5	✓ Clean	`CCC(=O)Nc1cc(C(=O)O)cc(C(=O)O)c1`
ZINC4826776 ZINC	0.556	380.4 Da LogP 1.77 TPSA 170.1	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)Nc1cc(NC(=O)CCCC(=O)O)cc(C(=O)O)c1`
ZINC8190075 ZINC	0.556	388.4 Da LogP 3.75 TPSA 95.5	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1)Nc1cc(NC(=O)Cc2ccccc2)cc(C(=O)O)c1`
ZINC4533843 ZINC	0.552	363.3 Da LogP -3.21 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533848 ZINC	0.552	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533853 ZINC	0.552	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)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.

KP13_01290

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

Chemistry

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence