KpATCC43816 Protein target profile

amidohydrolase, AtzE family protein

Accession: VK055_0719

Gene: AIK79342.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A483P6L7

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Length 465

Pocket druggability (P2Rank · AlphaFold DB model) 0.171

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 3 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.85. This is a computational pocket signal, not binding validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 3 structural and 0 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 38.065 Lower values reduce human off-target concern.
Human E-value: 5.5e-13
Gut microbiome similarity: 1.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 36.27 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.2 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) 0.171

Structure A0A483P6L7

Pocket Pocket 1

Druggability (FPocket) 0.853

Structure A0A483P6L7

Pocket Pocket 6

ColabFold model

P2Rank 0.176 · Pocket 1

FPocket 0.685 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 52 / 4744 genomes with a hit

Prevalence 1.1%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTLHHFTIAEIQRALHEGELSAREIARQTLDDIARVNPQINAWTEVTAQRMLAEADSIDALRREKRPLPPLAGIPYAVKNLFDVAGHTTLAGAELLSDRPPATSDSWAVRQLHSAGALLSGMLNMDAYAYGFTTENSHYGATRNPHDLSRIAGGSSGGSAAAVAAGLVHFSLGSDTNGSIRVPASLCGIFGLKPTFGRLSRSGSHPFVASLDHIGPFARRVADLAAVYDALQGRDPADDFQADKASERTGNLLDRGLEGLRCARLGGYFTTWCDDDARAAVDRVAHALGADSELQFADAALARSAAFIISASEGGNQYLTDLRHSPERFEPHSRERLLAGAMIPSAWYLQAQRFRRHARQAMKSLFSQADVLIAPATPCSATPIGAEEMVINGQPLPVRASMGMLTQPISFLGLPVVTVPLRTASGKPIGLQLIAAPFNEQACLRAARALEAMGITDARVAESAA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.3.5.-

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
1	453	SUPERFAMILY	SSF75304	Amidase signature (AS) enzymes
1	453	InterPro	IPR036928	Amidase signature (AS) superfamily
7	455	Gene3D	G3DSA:3.90.1300.10	Amidase signature (AS) domain
7	455	InterPro	IPR036928	Amidase signature (AS) superfamily
24	444	Pfam	PF01425	Amidase
24	444	InterPro	IPR023631	Amidase signature domain
4	452	PANTHER	PTHR11895	TRANSAMIDASE
4	452	InterPro	IPR000120	Amidase
8	456	NCBIfam	TIGR02715	AtzE family amidohydrolase
8	456	InterPro	IPR014087	1-carboxybiuret hydrolase, AtzE 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

0.171

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Surrounding area

Pocket 2 P2Rank #2

0.009

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Surrounding area

Pocket 3 P2Rank #3

0.009

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Surrounding area

Pocket 4 P2Rank #4

0.004

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #6

0.853

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Surrounding area

Pocket 2 FPocket #9

0.378

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Surrounding area

Pocket 3 FPocket #11

0.325

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.176

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Surrounding area

Pocket 2 P2Rank #2

0.044

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Surrounding area

Pocket 3 P2Rank #3

0.01

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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_A0A483P6L7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0719	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ACA PDB via homolog 131.2 Da · LogP 0.59 · TPSA 63.3 Open detail RCSB PDB

GJY PDB via homolog Detail RCSB PDB

UNU PDB via homolog Detail RCSB PDB

ZINC13357569 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1763117 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
ACA RCSB PDB	3A2Q	P13398	131.2 Da LogP 0.59 TPSA 63.3	✓ Ro5	✓ Clean	`C(CCC(=O)O)CCN`
GJY RCSB PDB	6DII	Q7XJJ7	344.5 Da LogP 7.38 TPSA 26.3	1 viol.	✓ Clean	`CC/C=C\C/C=C\C/C=C\CCCCCCCC[P@](=O)(OC)F`
UNU RCSB PDB	3A1I	Q7DKE4	121.1 Da LogP 0.79 TPSA 43.1	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)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
ZINC13357569 ZINC	1.000	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC1763117 ZINC	1.000	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1845814 ZINC	1.000	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)O`
ZINC22048354 ZINC	1.000	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCC(=O)O`
ZINC34552398 ZINC	1.000	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306 ZINC	1.000	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC3074822 ZINC	0.850	229.3 Da LogP 2.11 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCC(=O)CCCCCC(=O)O`
ZINC4822737 ZINC	0.850	313.5 Da LogP 4.45 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC3085979 ZINC	0.842	253.3 Da LogP 1.85 TPSA 77.2	✓ Ro5	Alert	`NC(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC1529497 ZINC	0.706	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.706	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.706	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.706	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.706	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.706	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.706	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC2390999 ZINC	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC13526937 ZINC	0.654	357.5 Da LogP 1.94 TPSA 121.5	✓ Ro5	✓ Clean	`NCCCCCC(=O)NCCCCCC(=O)NCCCCCC(=O)O`
ZINC1532906 ZINC	0.654	244.3 Da LogP 1.27 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCCCC(=O)NCCCCCC(=O)O`
ZINC40479778 ZINC	0.654	272.4 Da LogP 2.05 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCCCCC(=O)NCCCCCCC(=O)O`
ZINC13433578 ZINC	0.650	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC33433271 ZINC	0.625	213.2 Da LogP 2.58 TPSA 52.3	✓ Ro5	✓ Clean	`NC(=O)c1ccc(Oc2ccccc2)cc1`
ZINC59679948 ZINC	0.625	221.3 Da LogP 2.19 TPSA 43.1	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C#Cc2ccccc2)cc1`
ZINC71456227 ZINC	0.625	211.3 Da LogP 2.38 TPSA 43.1	✓ Ro5	✓ Clean	`NC(=O)c1ccc(Cc2ccccc2)cc1`
ZINC134027 ZINC	0.615	240.3 Da LogP 2.04 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc(NC(=O)c2ccccc2)cc1`
ZINC7690249 ZINC	0.615	241.2 Da LogP 2.00 TPSA 69.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(OC(=O)c2ccccc2)cc1`
ZINC1672966 ZINC	0.611	210.2 Da LogP 2.75 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1ccccc1)c1ccccc1`
ZINC116225 ZINC	0.600	255.3 Da LogP 2.43 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc(NC(=O)Nc2ccccc2)cc1`
ZINC12906734 ZINC	0.600	240.3 Da LogP 2.04 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C(=O)Nc2ccccc2)cc1`
ZINC132358 ZINC	0.600	240.3 Da LogP 1.55 TPSA 86.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc(-c2ccc(C(N)=O)cc2)cc1`
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`
ZINC26897400 ZINC	0.600	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.600	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.600	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.600	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.600	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC40470158 ZINC	0.593	216.3 Da LogP 0.49 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCC(=O)NCCCCCC(=O)O`
ZINC3055005 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC2391099 ZINC	0.586	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC36676 ZINC	0.583	225.2 Da LogP 2.02 TPSA 60.2	✓ Ro5	✓ Clean	`NC(=O)c1ccccc1C(=O)c1ccccc1`
ZINC100368719 ZINC	0.579	210.3 Da LogP 2.43 TPSA 52.0	✓ Ro5	✓ Clean	`N/C(=C(\N)c1ccccc1)c1ccccc1`
ZINC1590838 ZINC	0.579	342.4 Da LogP 3.82 TPSA 68.3	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1)c1ccccc1`
ZINC16133932 ZINC	0.579	474.5 Da LogP 4.88 TPSA 102.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccc(C(=O)C(=O)c3cccc…`
ZINC24716871 ZINC	0.579	210.3 Da LogP 2.43 TPSA 52.0	✓ Ro5	✓ Clean	`N/C(=C(/N)c1ccccc1)c1ccccc1`
ZINC204011879 ZINC	0.577	212.3 Da LogP 2.53 TPSA 55.1	✓ Ro5	✓ Clean	`NC(=O)c1cccc(Nc2ccccc2)c1`

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 A0A483P6L7