KpATCC43816 Protein target profile

ribosomal-protein-alanine acetyltransferase

Accession: VK055_2602

Gene: AIK81199.1 rimI 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GHX5

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Length 148

Pocket druggability (P2Rank · AlphaFold DB model) 0.852

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 66 total records

Functional annotation 1 EC 5 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.

Main supporting evidence

Second pocket predictor agrees P2Rank predicted binding-site probability 0.85. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 10 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 (%): 38.596 Lower values reduce human off-target concern.
Human E-value: 3.53e-07
Gut microbiome similarity: 2.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 84.459 Higher values support similarity to known essential genes.
DEG E-value: 2.36e-92 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.31 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) 0.852

Structure A0A0H3GHX5

Pocket Pocket 1

Druggability (FPocket) 0.405

Structure A0A0H3GHX5

Pocket Pocket 3

ColabFold model

P2Rank 0.897 · Pocket 1

FPocket 0.411 · Pocket 5

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 120 / 4744 genomes with a hit

Prevalence 2.5%

Metabolic context

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

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNTISTLSTADLTKAWHIEKRAHAFPWSEQTLASNQGERYRNYQLSVDGEMAAFAITQVVLDEATLFNIAVDPAYQRRGLGRALLEHVIDEVEKLGVVTLWLEVRASNVAAIALYESVGFNEATIRRNYYPTTDGREDAIIMALPISM

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.3.1.266

Gene Ontology (GO)

GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0006474 The acetylation of the N-terminal amino acid of proteins.
GO:0008080 Catalysis of the transfer of an acetyl group to a nitrogen atom on the acceptor molecule.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0008999 Catalysis of the reaction: acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H+ + N-terminal N(alpha)-acetyl-L-alanyl-[protein].

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
2	147	ProSiteProfiles	PS51186	Gcn5-related N-acetyltransferase (GNAT) domain profile.
2	147	InterPro	IPR000182	GNAT domain
48	103	CDD	cd04301	NAT_SF
11	142	NCBIfam	TIGR01575	ribosomal protein S18-alanine N-acetyltransferase
11	142	InterPro	IPR006464	N-acetyltransferase RimI/Ard1
1	148	Gene3D	G3DSA:3.40.630.30	-
17	120	Pfam	PF00583	Acetyltransferase (GNAT) family
17	120	InterPro	IPR000182	GNAT domain
33	143	PANTHER	PTHR43420	ACETYLTRANSFERASE
3	146	SUPERFAMILY	SSF55729	Acyl-CoA N-acyltransferases (Nat)
3	146	InterPro	IPR016181	Acyl-CoA N-acyltransferase
4	146	Hamap	MF_02210	[Ribosomal protein S18]-alanine N-acetyltransferase [rimI].
4	146	InterPro	IPR043690	N-acetyltransferase RimI
1	148	FunFam	G3DSA:3.40.630.30:FF:000018	[Ribosomal protein S18]-alanine N-acetyltransferase

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

0.852

Likely same site as FPocket 3 0.7 Å 29 shared residues 94% of smaller site

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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 #3

0.405 Unusual size

Likely same site as P2Rank 1 0.7 Å 29 shared residues 94% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:103-103 Proton acceptor

UniProt: Active site:115-115 Proton donor

UniProt: Binding site:108-108

UniProt: Binding site:69-71

UniProt: Binding site:77-82

Residue sets

UniProt: Active site:103-103 Proton acceptor

UniProt: Active site:115-115 Proton donor

UniProt: Binding site:108-108

UniProt: Binding site:69-71

UniProt: Binding site:77-82

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_A0A0H3GHX5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2602	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.

66 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 16 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 10 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CMC PDB via homolog 825.6 Da · LogP -1.78 · TPSA 383.9 Open detail RCSB PDB

TAR PDB via homolog Detail RCSB PDB

U2J PDB via homolog Detail RCSB PDB

U3V PDB via homolog Detail RCSB PDB

U3Y 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
CMC RCSB PDB	6Z00	Q9LFM3	825.6 Da LogP -1.78 TPSA 383.9	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…`
TAR RCSB PDB	5C82	Q08414	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)O)O`
U2J RCSB PDB	6WFK	Q9GZZ1	552.6 Da LogP -0.30 TPSA 195.3	1 viol.	✓ Clean	`CNC(=O)c1csc(n1)[C@@H]2C[C@@H](CN2C(=O)c3ccc(cc…`
U3V RCSB PDB	6WFG	Q9GZZ1	474.6 Da LogP 0.86 TPSA 125.4	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(n(n1)C)C(=O)N2CCC(CC2)C[C@@H](C(=O…`
U3Y RCSB PDB	6WFO	Q9GZZ1	552.6 Da LogP -0.30 TPSA 195.3	1 viol.	✓ Clean	`CNC(=O)c1csc(n1)[C@H]2C[C@@H](CN2C(=O)c3ccc(cc3…`
U44 RCSB PDB	6WF5	Q9GZZ1	262.4 Da LogP -0.05 TPSA 78.4	✓ Ro5	✓ Clean	`CC(C)(C)[C@H](C(=O)NCCC(=O)NCCS)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
CHEMBL4642700 ChEMBL	Q9GZZ1	7.89 ~12.9 nM	509.6 Da LogP 0.64 TPSA 166.2	1 viol.	✓ Clean	`Cc1csc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N(C)C(=…`
CHEMBL4642788 ChEMBL	Q9GZZ1	7.89 ~12.9 nM	552.6 Da LogP -0.30 TPSA 195.3	1 viol.	✓ Clean	`CNC(=O)c1csc(C2C[C@H](NC(=O)[C@@H]3CC(=O)N(C)C(…`
CHEMBL4639216 ChEMBL	Q9GZZ1	7.85 ~14.1 nM	536.5 Da LogP -0.77 TPSA 208.4	1 viol.	✓ Clean	`CNC(=O)c1coc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N…`
CHEMBL1230809 ChEMBL	Q9GZZ1	7.75 ~17.8 nM	809.6 Da LogP -1.32 TPSA 363.6	3 viol.	✓ Clean	`CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(=O)(O…`
CHEMBL4642911 ChEMBL	Q9GZZ1	7.52 ~30.2 nM	1223.1 Da LogP -2.50 TPSA 497.3	3 viol.	✓ Clean	`CSCC[C@H](NC(=O)CSCCNC(=O)CCNC(=O)[C@H](O)C(C)(…`
CHEMBL4644527 ChEMBL	Q9GZZ1	7.06 ~87.1 nM	538.6 Da LogP 0.05 TPSA 178.2	1 viol.	✓ Clean	`CNC(=O)c1csc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N…`
CHEMBL1213327 ChEMBL	Q9GZZ1	6.81 ~154.9 nM	767.5 Da LogP -1.67 TPSA 346.6	3 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)OC[C@H]1O[C@@H](n2cnc3…`
CHEMBL4636177 ChEMBL	Q9GZZ1	6.77 ~169.8 nM	485.5 Da LogP 1.16 TPSA 149.0	✓ Ro5	✓ Clean	`Cc1csc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N(C)C(=…`
CHEMBL4648534 ChEMBL	Q9GZZ1	6.37 ~426.6 nM	552.6 Da LogP -0.30 TPSA 195.3	1 viol.	✓ Clean	`CNC(=O)c1csc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N…`
CHEMBL4640907 ChEMBL	Q9GZZ1	6.00 ~1.0 µM	508.6 Da LogP 1.25 TPSA 153.3	1 viol.	✓ Clean	`Cc1csc([C@@H]2C[C@H](NC(=O)[C@@H]3CC(=O)N(C)C(=…`

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
ZINC3869683 ZINC	0.735	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](O)C(=O)NCCC(=O)NCCS`
ZINC3869684 ZINC	0.735	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCS`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC12501123 ZINC	0.547	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4228234 ZINC	0.547	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC79671662 ZINC	0.547	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC79671663 ZINC	0.547	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC1616450 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@@H]1CCCN1)[C@@H]1CCCN1`
ZINC5600257 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@H]1CCCN1`
ZINC8655607 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@@H]1CCCN1`
ZINC4899613 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974454 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC4974455 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974456 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC757216905 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@@H]([C@@H]2CCCNC2)CCN1`
ZINC757216906 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@H]([C@@H]2CCCNC2)CCN1`
ZINC757216908 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@@H]([C@H]2CCCNC2)CCN1`
ZINC757216910 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@H]([C@H]2CCCNC2)CCN1`
ZINC85223882 ZINC	0.513	261.3 Da LogP -2.05 TPSA 124.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCN`
ZINC12360002 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC1529331 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529332 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1529333 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529334 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@H](O)C(=O)O`
ZINC19409402 ZINC	0.500	224.3 Da LogP 1.97 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@@H]1CCCN1`
ZINC19409404 ZINC	0.500	224.3 Da LogP 1.97 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@H]1CCCN1`
ZINC74148205 ZINC	0.500	211.3 Da LogP 2.02 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@H](C2CCCCC2)CCN1`
ZINC74148208 ZINC	0.500	211.3 Da LogP 2.02 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@@H](C2CCCCC2)CCN1`
ZINC74148211 ZINC	0.500	211.3 Da LogP 2.02 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)[C@H]1C[C@H](C2CCCCC2)CCN1`
ZINC74148213 ZINC	0.500	211.3 Da LogP 2.02 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)[C@H]1C[C@@H](C2CCCCC2)CCN1`

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.

ribosomal-protein-alanine acetyltransferase

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways