KpATCC43816 Protein target profile

alpha amylase, catalytic domain protein

Accession: VK055_2210

Gene: AIK80816.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GJ07

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Length 605

Pocket druggability (P2Rank · AlphaFold DB model) 0.891

Direct ligand evidence 0 35 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.89. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 5 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 (%): 24.384 Lower values reduce human off-target concern.
Human E-value: 7.44e-15
Gut microbiome similarity: 1.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 42.5 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.07 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) 0.891

Structure A0A0H3GJ07

Pocket Pocket 1

Druggability (FPocket) 0.524

Structure A0A0H3GJ07

Pocket Pocket 5

ColabFold model

P2Rank 0.93 · Pocket 1

FPocket 0.321 · Pocket 36

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 81 / 4744 genomes with a hit

Prevalence 1.7%

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.

MLKAWHLPVAPFIKVQQDRLFITLWLSGESLPQRITLRAEEDNEELSLPMQRLRQAPQPGVVAWRGEISLASGQPRRRYSFKLLWADHQRWFTPQGFTRFPPARLEQFAIDLPDAGPQWVADQVFYQIFPDRFARSAARDADQDAVYYHHAAGREIVRKAWDDPLTGEAGGSTFYGGDLDGISEKLPYLKQLGVTALYLNPVFAAPSVHKYDTEDYRRVDPQFGGDAALLRLRHNTQRAGMRMILDGVFNHTGDSHPWFDRHQQGSGGAGHDPDSPWRDWFTFSEEGQAHNWLGYASLPKLDYRSTSLVNEIYAGEDSIVRHWLKAPWSMDGWRLDVVHMLGEGGGARNNLQHIAGITQAAKQAQPEAFVFGEHFGDARQWLQADAEDAAMNYRGFTFPIWGFLANTDISYDPQKIDAQTCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKSLLGKDVARLPLAVVWLFSWPGVPCIYYGDEVGVDGNNDPFCRKPFPWDPALQDTQLLALYQRMAKLRKAHQALRYGGCQVIYAEDNVVVFVRVYKQQRVLVAINRGEACEVVIEDSPLLNVAGWTLQEGAGAFQDGVLTLPAISANVWSGR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0004558 Catalysis of the hydrolysis of terminal, non-reducing alpha-(1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
GO:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
524	603	Gene3D	G3DSA:2.60.40.1180	-
524	603	InterPro	IPR013780	Glycosyl hydrolase, all-beta
122	531	CDD	cd11338	AmyAc_CMD
131	523	Gene3D	G3DSA:3.20.20.80	Glycosidases
127	521	SMART	SM00642	aamy
127	521	InterPro	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
530	603	SUPERFAMILY	SSF51011	Glycosyl hydrolase domain
117	530	SUPERFAMILY	SSF51445	(Trans)glycosidases
117	530	InterPro	IPR017853	Glycoside hydrolase superfamily
4	104	Pfam	PF02903	Alpha amylase, N-terminal ig-like domain
4	104	InterPro	IPR004185	Glycoside hydrolase, family 13, N-terminal Ig-like domain
177	493	Pfam	PF00128	Alpha amylase, catalytic domain
177	493	InterPro	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
94	570	PANTHER	PTHR10357	ALPHA-AMYLASE FAMILY MEMBER
1	601	PIRSF	PIRSF036918	Maltodextrin_glucosidase
1	601	InterPro	IPR017069	Maltodextrin glucosidase

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

0.891

Likely same site as FPocket 5 2.4 Å 17 shared residues 89% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.222

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Surrounding area

Pocket 3 P2Rank #3

0.163

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Surrounding area

Pocket 4 P2Rank #4

0.073

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Surrounding area

Pocket 5 P2Rank #5

0.01

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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 #5

0.524 Unusual size

Likely same site as P2Rank 1 2.4 Å 17 shared residues 89% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:336-336 Nucleophile

UniProt: Active site:373-373 Proton donor

UniProt: Site:448-448 Transition state stabilizer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.93

Likely same site as FPocket 36 5.4 Å 15 shared residues 88% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.366

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Surrounding area

Pocket 3 P2Rank #3

0.122

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Surrounding area

Pocket 4 P2Rank #4

0.077

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Surrounding area

Pocket 5 P2Rank #5

0.06

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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_A0A0H3GJ07	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2210	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.

35 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 30 similarity-based ZINC candidates

Best available ligand signal

ACG PDB via homolog 791.8 Da · LogP -9.71 · TPSA 380.1 Open detail RCSB PDB

ARE PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

NOJ PDB via homolog Detail RCSB PDB

PRU 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
ACG RCSB PDB	1LWJ	P80099	791.8 Da LogP -9.71 TPSA 380.1	3 viol.	✓ Clean	`C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@…`
ARE RCSB PDB	3A6O	Q08751	807.7 Da LogP -10.74 TPSA 400.3	3 viol.	✓ Clean	`C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@…`
FLC RCSB PDB	6WNI	U5CJP3	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
NOJ RCSB PDB	5WCZ	O06994	163.2 Da LogP -2.97 TPSA 93.0	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)O)O`
PRU RCSB PDB	3WY1	H3K096	290.3 Da LogP 0.75 TPSA 149.2	✓ Ro5	✓ Clean	`C[C@H](C[C@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O)C(…`

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
ZINC1690029 ZINC	0.600	204.2 Da LogP 0.42 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC(CCC(=O)O)C(=O)O`
ZINC100055151 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…`
ZINC100055153 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…`
ZINC100055156 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…`
ZINC100055157 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…`
ZINC2362797719 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@H]3[C@@H](O)[C…`
ZINC55537584 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)…`
ZINC103664702 ZINC	0.526	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@@H]2[C@@H](O)[C@@H](O)O[C@H…`
ZINC103664705 ZINC	0.526	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@@H]2[C@@H](O)[C@H](O)O[C@H]…`
ZINC16887664 ZINC	0.517	218.2 Da LogP 0.81 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC[C@@H](CCC(=O)O)C(=O)O`
ZINC16887665 ZINC	0.517	218.2 Da LogP 0.81 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC[C@H](CCC(=O)O)C(=O)O`
ZINC100352116 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@H…`
ZINC12358758 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@…`
ZINC13543637 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O[C@H]…`
ZINC13543975 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@…`
ZINC13544387 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@@…`
ZINC16051576 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@H]2[C@@H](CO)O[C@@H](O)[C@H…`
ZINC238808929 ZINC	0.509	828.7 Da LogP -11.92 TPSA 427.0	3 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O[C@@H]…`
ZINC238809271 ZINC	0.509	990.9 Da LogP -14.10 TPSA 506.1	3 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O[C@@H]…`
ZINC238809273 ZINC	0.509	990.9 Da LogP -14.10 TPSA 506.1	3 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O[C@@H]…`
ZINC245204745 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@H…`
ZINC4095490 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O)[C@H]…`
ZINC4261771 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@…`
ZINC43943076 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O[C@@…`
ZINC599389313 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@H]1O[C@H]…`
ZINC72283165 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O[C@@H]2[C@H](CO)O[C@H](O)[C@H]…`
ZINC16123955 ZINC	0.500	204.2 Da LogP -2.82 TPSA 101.8	✓ Ro5	✓ Clean	`CC(=O)NC[C@H]1NC[C@H](O)[C@@H](O)[C@@H]1O`
ZINC238808827 ZINC	0.500	853.8 Da LogP -10.75 TPSA 415.6	3 viol.	✓ Clean	`CC(=O)N[C@H]1[C@@H](O[C@H]2[C@@H](O)[C@@H](CO)O…`
ZINC64633908 ZINC	0.500	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2[C@@H](O)O[C@H](CO)[C@H]…`
ZINC64633910 ZINC	0.500	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@H]3O[C@H](CO…`

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 A0A0H3GJ07