KpKP13 Protein target profile

putative N-acetyltransferase

Accession: KP13_04477

Gene: AHE44351.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GP00

Export view

Length 180

Pocket druggability (P2Rank · AlphaFold DB model) 0.784

Direct ligand evidence 0 59 total records

Functional annotation 0 EC 1 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.78, FPocket 0.84). Use the 3D pocket comparison to verify whether they identify the same site. 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 0.84. This is a computational pocket signal, not binding validation. 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: 1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 82.84 Higher values support similarity to known essential genes.
DEG E-value: 1.85e-105 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.6 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) 0.784

Structure A0A0H3GP00

Pocket Pocket 1

Druggability (FPocket) 0.837

Structure A0A0H3GP00

Pocket Pocket 1

ColabFold model

P2Rank 0.83 · Pocket 1

FPocket 0.274 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 85 / 4744 genomes with a hit

Prevalence 1.8%

Sequence

Primary amino-acid sequence viewer.

MYEKLRFAMSIRPAIKDDCAAIAEIYNHAVVHTAAIWNDKTVDTDNRIAWFEARQLAGFPVLVSEEDGVITGYSSFGDWRAFDGFRHTVEHSVYVHPEHQGKGLGRKLLVALIAEARRLNKHVMVAGIESQNHASLHLHETLGFITTGQMPQVGTKFGRWLDLTFMQLQLDARQDPDGKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
61	125	CDD	cd04301	NAT_SF
33	144	Pfam	PF00583	Acetyltransferase (GNAT) family
33	144	InterPro	IPR000182	GNAT domain
10	174	PANTHER	PTHR43072	N-ACETYLTRANSFERASE
8	179	FunFam	G3DSA:3.40.630.30:FF:000026	Phosphinothricin acetyltransferase
7	179	Gene3D	G3DSA:3.40.630.30	-
9	171	ProSiteProfiles	PS51186	Gcn5-related N-acetyltransferase (GNAT) domain profile.
9	171	InterPro	IPR000182	GNAT domain
11	172	SUPERFAMILY	SSF55729	Acyl-CoA N-acyltransferases (Nat)
11	172	InterPro	IPR016181	Acyl-CoA N-acyltransferase

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.784

Likely same site as FPocket 1 0.7 Å 24 shared residues 96% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.467

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.074

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.009

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

0.837 Unusual size

Likely same site as P2Rank 1 0.7 Å 24 shared residues 96% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #2

0.292

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.83

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.347

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.032

Show in viewer

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_A0A0H3GP00	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04477	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

AZI PDB via homolog 42.0 Da · LogP 0.87 · TPSA 58.7 Open detail RCSB PDB

BLJ PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

HLG PDB via homolog Detail RCSB PDB

NHE 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
AZI RCSB PDB	2JLM	Q6FBS8	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BLJ RCSB PDB	5WPH	Q88LK7	225.1 Da LogP -0.72 TPSA 100.6	✓ Ro5	✓ Clean	`C[As](=O)(CC[C@@H](C(=O)O)N)O`
FLC RCSB PDB	4JXQ	Q92L60	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
HLG RCSB PDB	6E1X	Q9KL03	187.3 Da LogP -0.16 TPSA 67.2	✓ Ro5	✓ Clean	`CC(=O)NCCCNCCCCN`
NHE RCSB PDB	4NCZ	Q9KL03	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
PPQ RCSB PDB	6M7G	Q88LK7	181.1 Da LogP -0.31 TPSA 100.6	✓ Ro5	✓ Clean	`C[P@](=O)(CC[C@@H](C(=O)O)N)O`
SP5 RCSB PDB	6E1X	Q9KL03	244.4 Da LogP -0.18 TPSA 79.2	✓ Ro5	✓ Clean	`CC(=O)NCCCNCCCCNCCCN`
SPD RCSB PDB	4MHD	Q9KL03	145.2 Da LogP -0.34 TPSA 64.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CN`
SPM RCSB PDB	4MI4	Q9KL03	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CNCCCN`

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
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC27564039 ZINC	0.933	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742 ZINC	0.929	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC1532734 ZINC	0.929	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC3870097 ZINC	0.920	244.4 Da LogP -0.18 TPSA 79.2	✓ Ro5	✓ Clean	`CC(=O)NCCCNCCCCNCCCN`
ZINC1598087 ZINC	0.867	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC3130432 ZINC	0.800	214.4 Da LogP 2.20 TPSA 55.1	✓ Ro5	✓ Clean	`CC(=O)NCCCCCCCCCCN`
ZINC1650371 ZINC	0.792	229.3 Da LogP 0.02 TPSA 70.2	✓ Ro5	✓ Clean	`CC(=O)NCCCCNCCCNC(C)=O`
ZINC4096102 ZINC	0.792	286.4 Da LogP -0.00 TPSA 82.3	✓ Ro5	✓ Clean	`CC(=O)NCCCNCCCCNCCCNC(C)=O`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC100056474 ZINC	0.650	270.5 Da LogP 4.63 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNCCCN`
ZINC107767463 ZINC	0.650	200.4 Da LogP 2.68 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCNCCCCCCN`
ZINC59496006 ZINC	0.650	242.5 Da LogP 3.85 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNCCCN`
ZINC526059846 ZINC	0.645	257.4 Da LogP 0.93 TPSA 84.2	✓ Ro5	✓ Clean	`CC(=O)NCCCCCCNC(=O)CCCCN`
ZINC34514995 ZINC	0.606	245.4 Da LogP 1.23 TPSA 76.4	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)NCCCNCCCCN`
ZINC1530428 ZINC	0.600	323.3 Da LogP -1.30 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](C)NC(=O)[C@@H](N)CC[P@](C)(=…`
ZINC1587088 ZINC	0.600	214.3 Da LogP 1.21 TPSA 58.2	✓ Ro5	✓ Clean	`CC(=O)NCCCCCCCNC(C)=O`
ZINC1615894 ZINC	0.600	200.3 Da LogP 0.82 TPSA 58.2	✓ Ro5	✓ Clean	`CC(=O)NCCCCCCNC(C)=O`
ZINC4958190 ZINC	0.600	256.4 Da LogP 2.38 TPSA 58.2	✓ Ro5	✓ Clean	`CC(=O)NCCCCCCCCCCNC(C)=O`
ZINC5882912 ZINC	0.600	323.3 Da LogP -1.30 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](N)CC[P@](C)(=O…`
ZINC34275204 ZINC	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@](C)(=O)CC[C@H](N)C(=O)O`
ZINC34275205 ZINC	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@@](C)(=O)CC[C@H](N)C(=O)O`
ZINC34275206 ZINC	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@](C)(=O)CC[C@@H](N)C(=O)O`
ZINC34275207 ZINC	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@@](C)(=O)CC[C@@H](N)C(=O)O`
ZINC20112395 ZINC	0.581	239.2 Da LogP -0.47 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CC[P@](=O)(O)CCC(=O)O)C(=O)O`
ZINC20112808 ZINC	0.567	211.2 Da LogP -0.25 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCP(=O)(O)O)C(=O)O`
ZINC2169486 ZINC	0.567	211.2 Da LogP -0.25 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCP(=O)(O)O)C(=O)O`
ZINC22465713 ZINC	0.563	232.4 Da LogP -2.74 TPSA 100.2	1 viol.	✓ Clean	`NCCNCCNCCNCCNCCN`
ZINC19367005 ZINC	0.560	224.4 Da LogP 2.83 TPSA 24.1	✓ Ro5	✓ Clean	`C1CCC(NCCNC2CCCCC2)CC1`
ZINC26468763 ZINC	0.559	243.3 Da LogP -1.35 TPSA 100.5	✓ Ro5	✓ Clean	`O=S(=O)(O)CCN[C@@H]1CCS(=O)(=O)C1`
ZINC26468770 ZINC	0.559	243.3 Da LogP -1.35 TPSA 100.5	✓ Ro5	✓ Clean	`O=S(=O)(O)CCN[C@H]1CCS(=O)(=O)C1`
ZINC5188799 ZINC	0.556	280.5 Da LogP 4.39 TPSA 24.1	✓ Ro5	✓ Clean	`C(CCCNC1CCCCC1)CCNC1CCCCC1`
ZINC31361891 ZINC	0.550	200.3 Da LogP -0.58 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNC/C=C/CNCCCN`
ZINC4978005 ZINC	0.550	200.3 Da LogP -0.58 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNC/C=C\CNCCCN`
ZINC1856281 ZINC	0.548	225.2 Da LogP 0.14 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCCP(=O)(O)O)C(=O)O`
ZINC2149821 ZINC	0.548	239.2 Da LogP 0.53 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCP(=O)(O)O)C(=O)O`
ZINC2149823 ZINC	0.548	239.2 Da LogP 0.53 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCCCP(=O)(O)O)C(=O)O`
ZINC2516019 ZINC	0.548	225.2 Da LogP 0.14 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCCP(=O)(O)O)C(=O)O`
ZINC4991083 ZINC	0.548	385.6 Da LogP 1.41 TPSA 122.3	✓ Ro5	✓ Clean	`NCCCC(=O)NCCCCCCNCCCCCCNC(=O)CCCN`
ZINC169723055 ZINC	0.542	228.3 Da LogP 1.00 TPSA 98.8	✓ Ro5	Alert	`[N-]=[N+]=NCCCNCCCCNCCCN`
ZINC96031411 ZINC	0.538	230.3 Da LogP -1.56 TPSA 82.3	✓ Ro5	✓ Clean	`CC(=O)NCCNCCNCCNC(C)=O`
ZINC2168583 ZINC	0.529	237.3 Da LogP 0.16 TPSA 86.6	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@@H](O)CNC1CCCCC1`
ZINC2168584 ZINC	0.529	237.3 Da LogP 0.16 TPSA 86.6	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@H](O)CNC1CCCCC1`
ZINC12887775 ZINC	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](C[P@@](=O)(O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC4089897 ZINC	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@@H](C[P@](=O)(O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4089900 ZINC	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](C[P@](=O)(O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC100638283 ZINC	0.524	200.4 Da LogP 2.68 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCNCCN`
ZINC100967545 ZINC	0.524	256.5 Da LogP 4.24 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNCCN`
ZINC1857785994 ZINC	0.520	271.5 Da LogP -0.33 TPSA 70.5	✓ Ro5	✓ Clean	`NCCCCNCCN1CCN(CCCCN)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.

Cross-references

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

Sequence

UniProt A0A0H3GP00