KpKP13 Protein target profile

Aspartate carbamoyltransferase regulatory chain

Accession: KP13_01289

Gene: pyrI AHE46645.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLQ7

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Length 153

Pocket druggability (P2Rank · AlphaFold DB model) 0.035

Direct ligand evidence 0 52 total records

Functional annotation 0 EC 2 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.79. This is a computational pocket signal, not binding validation. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for 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: No hit
Gut microbiome similarity: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 62.0 Higher values support similarity to known essential genes.
DEG E-value: 1.4599999999999999e-67 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 89.69 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) 0.035

Structure A0A0H3GLQ7

Pocket Pocket 1

Druggability (FPocket) 0.787

Structure A0A0H3GLQ7

Pocket Pocket 1

ColabFold model

P2Rank 0.086 · Pocket 1

FPocket 0.284 · Pocket 6

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 127 / 4744 genomes with a hit

Prevalence 2.7%

Cross-references

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

Sequence

UniProt A0A0H3GLQ7

Sequence

Primary amino-acid sequence viewer.

MTHDNKLQVEAIKRGTVIDHIPAQVGFKLLTLFKLTETDQRITIGLNLPSGEMGRKDLIKIENTFLTDEQVNQLSLYAPQATVNRIDDYEVVGKSRPSLPDRIDSVLVCPNSNCISHAEPVSSSFAVKKRADDIALKCKYCEKEFSHYVVLAN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Subcellular localization

Localization: Cytoplasmic

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:0009347 A multienzyme complex that catalyzes the formation N-carbamoyl-L-aspartate from carbamoyl phosphate and L-aspartate. It exhibits a variety of architectural organizations, but in all microorganisms the core catalytic component is a homotrimer of approximately 34 kDa polypeptides.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
2	100	FunFam	G3DSA:3.30.70.140:FF:000001	Aspartate carbamoyltransferase regulatory chain
102	147	Pfam	PF02748	Aspartate carbamoyltransferase regulatory chain, metal binding domain
102	147	InterPro	IPR020542	Aspartate carbamoyltransferase regulatory subunit, C-terminal
102	150	SUPERFAMILY	SSF57825	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain
102	150	InterPro	IPR036792	Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily
101	153	FunFam	G3DSA:2.30.30.20:FF:000001	Aspartate carbamoyltransferase regulatory chain
4	152	Hamap	MF_00002	Aspartate carbamoyltransferase regulatory chain [pyrI].
4	152	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit
2	100	SUPERFAMILY	SSF54893	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain
2	100	InterPro	IPR036793	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily
101	153	Gene3D	G3DSA:2.30.30.20	-
1	151	PANTHER	PTHR35805	ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN
1	151	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit
7	96	Pfam	PF01948	Aspartate carbamoyltransferase regulatory chain, allosteric domain
7	96	InterPro	IPR020545	Aspartate carbamoyltransferase regulatory subunit, N-terminal
1	100	Gene3D	G3DSA:3.30.70.140	-
1	100	InterPro	IPR036793	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily
5	152	NCBIfam	TIGR00240	aspartate carbamoyltransferase regulatory subunit
5	152	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit

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

0.035

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.787

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:109-109

UniProt: Binding site:114-114

UniProt: Binding site:138-138

UniProt: Binding site:141-141

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_A0A0H3GLQ7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01289	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DCP PDB via homolog 467.2 Da · LogP -1.18 · TPSA 250.2 Open detail RCSB PDB

PAL PDB via homolog Detail RCSB PDB

ZINC12503365 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC13435050 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1563934 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
DCP RCSB PDB	4FYX	P0A7F3	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
PAL RCSB PDB	1I5O	P0A7F3	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`

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
ZINC12503365 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13435050 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
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`
ZINC8215945 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC13435042 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC142514175 ZINC	0.818	483.2 Da LogP 0.19 TPSA 233.1	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC12503923 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532581 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3645374 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861759 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869816 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC71404913 ZINC	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O[P@@](=O)(O)OC[C@H]1O[C@@H](n2ccc(N…`
ZINC71404916 ZINC	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O)O[P@@](C)(=O)O[P@@](=O)(O)OC[C@H]1…`
ZINC8215971 ZINC	0.796	468.1 Da LogP -1.06 TPSA 244.4	2 viol.	✓ Clean	`O=c1nc(O)ccn1[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC169292613 ZINC	0.750	492.2 Da LogP 0.14 TPSA 278.7	1 viol.	Alert	`[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(N)nc2=O)O[C@@H]1…`
ZINC111437949 ZINC	0.741	481.2 Da LogP -0.72 TPSA 236.2	2 viol.	✓ Clean	`CNc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P…`
ZINC13516800 ZINC	0.737	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@H]2CC[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC32016993 ZINC	0.737	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CC[C@H](CO[P@@](=O)(O)O[P@](=O)(O…`
ZINC12502055 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC218114467 ZINC	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC31440313 ZINC	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC142487928 ZINC	0.719	483.2 Da LogP -1.48 TPSA 270.4	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)…`
ZINC13588928 ZINC	0.712	469.2 Da LogP -0.24 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CS[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC104864216 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC58633440 ZINC	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC62612120 ZINC	0.695	481.2 Da LogP -0.87 TPSA 250.2	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC81982895 ZINC	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC81982899 ZINC	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`

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.