KpKP13 Protein target profile

Maltose O-acetyltransferase

Accession: KP13_03634

Gene: maa AHE45976.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GKK7

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Length 188

Pocket druggability (P2Rank · AlphaFold DB model) 0.078

Direct ligand evidence 0 33 total records

Functional annotation 0 EC 4 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

Risks to review

Microbiome similarity 195 of 4744 screened genomes (4.1%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.12. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.08.

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: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 41.509 Higher values support similarity to known essential genes.
DEG E-value: 9.91e-30 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.32 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) 0.078

Structure A0A0H3GKK7

Pocket Pocket 1

Druggability (FPocket) 0.123

Structure A0A0H3GKK7

Pocket Pocket 6

ColabFold model

P2Rank 0.111 · Pocket 1

FPocket 0.369 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 195 / 4744 genomes with a hit

Prevalence 4.1%

Sequence

Primary amino-acid sequence viewer.

MSEEKRKMIAGELYLSGDPTLRADRLRARQLLHRYNHSAPDDQEQRQHILAELFARAGDAYIEPSFRCDYGYNIFLGAGFYANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDADARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPACTVVGGNPAQIIKRLPPTNP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0016407 Catalysis of the transfer of an acetyl group to an acceptor molecule.
GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0016413 Catalysis of the transfer of an acetyl group to an oxygen atom on the acceptor molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
92	109	Pfam	PF14602	Hexapeptide repeat of succinyl-transferase
92	109	InterPro	IPR001451	Hexapeptide repeat
129	164	Pfam	PF14602	Hexapeptide repeat of succinyl-transferase
129	164	InterPro	IPR001451	Hexapeptide repeat
2	183	SUPERFAMILY	SSF51161	Trimeric LpxA-like enzymes
2	183	InterPro	IPR011004	Trimeric LpxA-like superfamily
13	180	CDD	cd03357	LbH_MAT_GAT
5	59	SMART	SM01266	Mac_2
5	59	InterPro	IPR024688	Maltose/galactoside acetyltransferase
7	58	Pfam	PF12464	Maltose acetyltransferase
7	58	InterPro	IPR024688	Maltose/galactoside acetyltransferase
138	166	ProSitePatterns	PS00101	Hexapeptide-repeat containing-transferases signature.
138	166	InterPro	IPR018357	Hexapeptide transferase, conserved site
1	183	Gene3D	G3DSA:2.160.10.10	Hexapeptide repeat proteins
3	185	PANTHER	PTHR23416	SIALIC ACID SYNTHASE-RELATED
1	184	FunFam	G3DSA:2.160.10.10:FF:000008	Maltose O-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.

Download VMD script Full viewer

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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

0.078

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_A0A0H3GKK7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03634	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.

33 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 27 similarity-based ZINC candidates

Best available ligand signal

B2M PDB via homolog 453.1 Da · LogP 5.08 · TPSA 74.6 Open detail RCSB PDB

DCA PDB via homolog Detail RCSB PDB

DOL PDB via homolog Detail RCSB PDB

PBM PDB via homolog Detail RCSB PDB

SOP 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
B2M RCSB PDB	3DHO	P50870	453.1 Da LogP 5.08 TPSA 74.6	1 viol.	Alert	`Cc1cc(c2cc(ccc2n1)Br)C(=O)N/N=C\c3cc(cc(c3O)Cl)…`
DCA RCSB PDB	2XAT	P26841	735.5 Da LogP -1.58 TPSA 346.6	3 viol.	✓ Clean	`CCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@@](=O)(O)O[P…`
DOL RCSB PDB	1MRL	P50870	690.9 Da LogP 2.27 TPSA 176.4	2 viol.	✓ Clean	`CCN(CC)CCS(=O)(=O)[C@@H]1CCN2[C@H]1C(=O)O[C@@H]…`
PBM RCSB PDB	1OCX	P77791	252.3 Da LogP 1.37 TPSA 0.0	✓ Ro5	✓ Clean	`C[Pb+](C)C`
SOP RCSB PDB	2WLG	Q93S40	823.6 Da LogP -1.27 TPSA 363.6	3 viol.	✓ Clean	`CC(=O)CSCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O…`
SXA RCSB PDB	6X3C	P26839	400.4 Da LogP -0.61 TPSA 162.3	✓ Ro5	✓ Clean	`CC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C)COP(=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).

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
ZINC69350237 ZINC	0.574	279.1 Da LogP 2.67 TPSA 42.0	✓ Ro5	✓ Clean	`CNC(=O)c1cc(C)nc2ccc(Br)cc12`
ZINC254341325 ZINC	0.559	429.2 Da LogP 3.68 TPSA 117.7	✓ Ro5	Alert	`Cc1cc(C(=O)NN=Cc2cc(Br)cc([N+](=O)[O-])c2O)c2cc…`
ZINC12501123 ZINC	0.553	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	0.553	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	0.553	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	0.553	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…`
ZINC751088093 ZINC	0.531	432.7 Da LogP 4.57 TPSA 71.1	✓ Ro5	✓ Clean	`CNC(=O)c1cc(Cl)ccc1NC(=O)c1cc(C)nc2ccc(Br)cc12`
ZINC69570560 ZINC	0.517	295.1 Da LogP 2.60 TPSA 51.2	✓ Ro5	✓ Clean	`CONC(=O)c1cc(C)nc2ccc(Br)cc12`
ZINC12360002 ZINC	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	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	0.511	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC1662516 ZINC	0.511	232.3 Da LogP -0.09 TPSA 75.3	✓ Ro5	✓ Clean	`CC(=O)NCCC(=O)NCCSC(C)=O`
ZINC69061 ZINC	0.509	266.1 Da LogP 3.00 TPSA 50.2	✓ Ro5	✓ Clean	`Cc1cc(C(=O)O)c2cc(Br)ccc2n1`
ZINC3871401 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC14140797 ZINC	0.500	311.2 Da LogP 3.55 TPSA 70.4	✓ Ro5	Alert	`Cc1cc(C)nc(N/N=C/c2cc(Cl)cc(Cl)c2O)n1`

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 A0A0H3GKK7

Maltose O-acetyltransferase

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence